Relevant bibliographies by topics / High protein

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'High protein'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 August 2024

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Journal articles on the topic "High protein"

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Gray, Jeffrey J. "High-resolution protein–protein docking." Current Opinion in Structural Biology 16, no. 2 (April 2006): 183–93. http://dx.doi.org/10.1016/j.sbi.2006.03.003.

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Huang, Yongqi, and Zhirong Liu. "Do Intrinsically Disordered Proteins Possess High Specificity in Protein-Protein Interactions?" Chemistry - A European Journal 19, no. 14 (February 21, 2013): 4462–67. http://dx.doi.org/10.1002/chem.201203100.

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Shirai, T., A. Suzuki, T. Yamane, T. Ashida, T. Kobayashi, J. Hitomi, and S. Ito. "High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism." Protein Engineering Design and Selection 10, no. 6 (June 1, 1997): 627–34. http://dx.doi.org/10.1093/protein/10.6.627.

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Nakasako, Masayoshi. "Water–protein interactions from high–resolution protein crystallography." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, no. 1448 (August 29, 2004): 1191–206. http://dx.doi.org/10.1098/rstb.2004.1498.

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To understand the role of water in life at molecular and atomic levels, structures and interactions at the protein–water interface have been investigated by cryogenic X–ray crystallography. The method enabled a much clearer visualization of definite hydration sites on the protein surface than at ambient temperature. Using the structural models of proteins, including several hydration water molecules, the characteristics in hydration structures were systematically analysed for the amount, the interaction geometries between water molecules and proteins, and the local and global distribution of water molecules on the surface of proteins. The tetrahedral hydrogen–bond geometry of water molecules in bulk solvent was retained at the interface and enabled the extension of a three–dimensional chain connection of a hydrogen–bond network among hydration water molecules and polar protein atoms over the entire surface of proteins. Networks of hydrogen bonds were quite flexible to accommodate and/or to regulate the conformational changes of proteins such as domain motions. The present experimental results may have profound implications in the understanding of the physico–chemical principles governing the dynamics of proteins in an aqueous environment and a discussion of why water is essential to life at a molecular level.
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Scholtens, Denise, and Robert Gentleman. "Making Sense of High-Throughput Protein-Protein Interaction Data." Statistical Applications in Genetics and Molecular Biology 3, no. 1 (January 3, 2005): 1–31. http://dx.doi.org/10.2202/1544-6115.1107.

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Accurate systems biology modeling requires a complete catalog of protein complexes and their constituent proteins. We discuss a graph-theoretic/statistical algorithm for local dynamic modeling of protein complexes using data from affinity purification-mass spectrometry experiments. The algorithm readily accommodates multicomplex membership by individual proteins and dynamic complex composition, two biological realities not accounted for in existing topological descriptions of the overall protein network. A likelihood-based objective function guides the protein complex modeling algorithm. With an accurate complex membership catalog in place, systems biology can proceed with greater precision.
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Khait, R., and G. Schreiber. "FRETex: a FRET-based, high-throughput technique to analyze protein-protein interactions." Protein Engineering Design and Selection 25, no. 11 (September 25, 2012): 681–87. http://dx.doi.org/10.1093/protein/gzs067.

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Becher, Karen, and Julie Prinsen. "High-Protein Cereals." Journal of Renal Nutrition 17, no. 5 (September 2007): e37-e38. http://dx.doi.org/10.1053/j.jrn.2007.06.003.

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Baderman, Natalie. "High-protein spaghetti." Trends in Biotechnology 19, no. 10 (October 2001): 381. http://dx.doi.org/10.1016/s0167-7799(01)01838-8.

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Brown, Laura D., Kendra Hendrickson, Marc L. Masor, and William W. Hay. "High-Protein Formulas." Clinics in Perinatology 41, no. 2 (June 2014): 383–403. http://dx.doi.org/10.1016/j.clp.2014.02.002.

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Patel, Dr Vihang B., Dr Haresh Panchal, and DR BHAVESH Patel. "Study of High Sensitive C Reactive Protein [HsCRP] in Obesity." International Journal of Scientific Research 1, no. 7 (June 1, 2012): 152–53. http://dx.doi.org/10.15373/22778179/dec2012/55.

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Dissertations / Theses on the topic "High protein"

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Jüttemann, Thomas. "Adding 3D-structural context to protein-protein interaction data from high-throughput experiments." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/5666.

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In the past decade, automatisation has led to an immense increase of data in biology. Next generation sequencing techniques will produce a vast amount of sequences across all species in the coming years. In many cases, identifying the function and biological role of a protein from its sequence can be a complicated and time-intensive task. The identification of a protein's interaction partners is a tremendous help for understanding the biological context in which it is involved. In order to fully characterise a protein-protein interaction (PPIs), it is necessary to know the three-dimensional structure of the interacting partners. Despite optimisation efforts from projects such as the Protein Structure Initivative, determining the structure of a protein through crystallography remains a time- and cost-intensive procedure. The primary aim of the research described in this dissertation was to produce a World Wide Web resource that facilitates visual exploration and validation (or questioning) of data derived from functional genomics experiments, by building upon existing structural information about direct physical PPIs. Secondary aims were (i) to demonstrate the utility of the new resource, and (ii) its application in biological research. We created a database that emphasises specifically the intersection between the PPIs-results emerging from the structural biology and functional genomics communities. The BISC database holds BInary SubComplexes and Modellable Interactions in current functional genomics databases (BICS-MI). It is publicly available at hyyp://bisc.cse.ucsc.edu. BISC is divided in three sections that deliver three types of information of interest to users seeking to investigate or browse PPIs. The template section (BISCHom and BISCHet) is devoted to those PPIs that are characterised in structural detail, i.e. binary SCs extracted from experimentally determined three-dimensional structures. BISCHom and BISCHet contain the homodimeric (13,583 records) and heterodimeric (5612 records) portions of these, respectively. Besides interactive, embedded Jmol displays emphasising the interface, standard information and links are provided, e.g. sequence information and SPOP classification for both partners, interface size and energy scores (PISA). An automated launch of the MolSurfer program enables the user to investigate electrostatic and hydrophobic correlation between the partners, at the inter-molecular interface. The modellable interactions section (BISC0MI) identifies potentially modellable interactions in three major functional genomics interaction databases (BioGRID), IntAct, HPRD). To create BISC-MI all PPIs that are amenable to automated homology modelling based on conservative similarity cut-offs and whose partner protein sequences have recrods in the UniProt database, have been extracted. The modellable interaction services (BISC-MI Services) section offers, upon user request, modelled SC-structures for any PPIs in BISC-MI. This is enabled through an untomated template-based (homology) modelling protocol using the popular MODELLER program. First, a multiple sequence alignment (MSA) is generated using MUSCLE, between the target and homologous proteins collected from UniProt (only reviewed proteins from organisms whose genome has been completely sequenced are included to find putative orthologs). Then a sequence-to-profile alignment is generated to integrate the template structure in the MSA. All models are produced upon user request to ensure that the most recent sequence data for the MSAs are used. Models generated through this protocol are expected to be more accurate generally than models offered by other automated resources that rely on pairwise alignments, e.g. ModBase. Two small studies were carried out to demonstrate the usability and utility of BISC in biological research. (1) Interaction data in functional genomics databases often suffers from insufficient experimental and reporting standards. For example, multiple protein complexes are typically recorded as an inferred set of binary interactions. Using the 20S core particle of the yeast proteasome as an example, we demonstrate how the BISC Web resource can be used as a starting point for further investigation of such inferred interactions. (2) Malaria, a mosquito-borne disease, affects 3500-500 million people worldwide. Still very little is known about the malarial parasites' genes and their protein functions. For Plasmodium falciparum, the most lethal among the malaria parasites, only one experimentally derived medium scale PPIs set is available. The validity of this set has been doubted in the the malarial biologist community. We modelled and investigated eleven binary interactions from this set using the BISC modelling pipeline. Alongside we compared the BISC models of the individual partners to those obtained from ModBase.
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Díaz, Maria Dolores Fernández. "Effects of high pressure on protein protein interactions." Thesis, University of Reading, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270415.

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Leuchowius, Karl-Johan. "High Content Analysis of Proteins and Protein Interactions by Proximity Ligation." Doctoral thesis, Uppsala universitet, Molekylära verktyg, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-119530.

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Fundamental to all biological processes is the interplay between biomolecules such as proteins and nucleic acids. Studies of interactions should therefore be more informative than mere detection of expressed proteins. Preferably, such studies should be performed in material that is as biologically and clinically relevant as possible, i.e. in primary cells and tissues. In addition, to be able to take into account the heterogeneity of such samples, the analyses should be performed in situ to retain information on the sub-cellular localization where the interactions occur, enabling determination of the activity status of individual cells and allowing discrimination between e.g. tumor cells and surrounding stroma. This requires assays with an utmost level of sensitivity and selectivity. Taking these issues into consideration, the in situ proximity-ligation assay (in situ PLA) was developed, providing localized detection of proteins, protein-protein interactions and post-translational modifications in fixed cells and tissues. The high sensitivity and selectivity afforded by the assay's requirement for dual target recognition in combination with powerful signal amplification enables visualization of single protein molecules in intact single cells and tissue sections. To further increase the usefulness and application of in situ PLA, the assay was adapted to high content analysis techniques such as flow cytometry and high content screening. The use of in situ PLA in flow cytometry offers the possibility for high-throughput analysis of cells in solution with the unique characteristics offered by the assay. For high content screening, it was demonstrated that in situ PLA can enable cell-based drug screening of compounds affecting post-translational modifications and protein-protein interactions in primary cells, offering superior abilities over current assays. The methods presented in this thesis provide powerful new tools to study proteins in genetically unmodified cells and tissues, and should offer exciting new possibilities for molecular biology, diagnostics and drug discovery. 
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Cummings, Chad S. "High Density Polymer Modification of Proteins Using Polymer - Based Protein Engineering." Research Showcase @ CMU, 2016. http://repository.cmu.edu/dissertations/692.

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Proteins and protein-based materials are used for a wide range of therapeutic, diagnostic, and biotechnological applications. Still, the inherent instability of proteins in non-native environments greatly limits the applications in which they are effective. In order to increase their utility, proteins are often modified, either biologically or chemically, to manipulate their bioactivity and stability profiles. In this work, covalent attachment of polymers to the enzyme chymotrypsin was used to predictably tailor protein bioactivity and stability. Specifically, atom transfer radical polymerization (ATRP) based polymer-based protein engineering (PBPE) was used to grow polymers directly from the surface of chymotrypsin. First, the temperature responsive polymers poly(N-isopropyl acrylamide) (pNIPAM), which has a lower critical solution temperature (LCST) and poly(dimethylamino propane sulfonate) (pDMAPS), which has an upper critical solution temperature (UCST), were separately grown from chymotrypsin. The temperature responsive properties of the polymers were conserved in the protein-polymer conjugates, and chymotrypsin bioactivity, productivity, and substrate specificity were predictably tailored at different temperatures depending on the structural organization of the polymers. Next, a dual block polymer-chymotrypsin conjugate was synthesized by growing poly(sulfobetaine methacrylamide) (pSBAm)-block-pNIPAm conjugates from the surface of chymotrypsin. The CT-pSBAm-b-pNIPAm conjugates showed temperature dependent kinetics, due to UCST or LCST driven polymer collapse at high and low temperature. Most interestingly, the dual block conjugates were dramatically more stable than native chymotrypsin to low pH. In order to further investigate the effect of polymer conjugation on chymotrypsin stability at low pH, four distinct and uniquely charged polymers were grown from the surface of chymotrypsin. With these new conjugates, we confirmed that chymotrypsin low pH stability was dependent on the chemical structure of polymers covalently attached to chymotrypsin. Indeed, positively charged polymers stabilized chymotrypsin to low pH, but negatively charged and amphiphilic polymers destabilized the enzyme. Lastly, after developing strategies for low pH stabilization, new protein-polymer conjugates with the chemical permeation enhancer 1-phenylpiperazine were designed to enable protein transport across the intestinal epithelium. Bovine serum albumin-poly(oligoethylene methacrylate)-block-poly(phenylpiperazine acrylamide) BSA-pOEGMA-b-pPPZ conjugates induced dose dependent increases in Caco-2 monolayer permeability and transported across an in vitro intestinal monolayer model with low cell toxicity.
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Faupel, Thomas. "Identification of protein-protein-interactions in vitro based on high-density protein arrays." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972661077.

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Friedel, Caroline Christina. "Analysis of High-Throughput Data - Protein-Protein Interactions, Protein Complexes and RNA Half-life." Diss., lmu, 2009. http://nbn-resolving.de/urn:nbn:de:bvb:19-96883.

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Pandey, Bikesh. "Analysis of Protein-Protein Interaction Networks Using High Performance Scalable Tools." ScholarWorks@UNO, 2018. https://scholarworks.uno.edu/honors_theses/113.

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Protein-Protein Interaction (PPI) Research currently generates an extraordinary amount of publications and interest in fellow computer scientists and biologists alike because of the underlying potential of the source material that researchers can work with. PPI networks are the networks of protein complexes formed by biochemical events or electrostatic forces serving a biological function [1]. Since the analysis of the protein networks is now growing, we have more information regarding protein, genomes and their influence on life. Today, PPI networks are used to study diseases, improve drugs and understand other processes in medicine and health that will eventually help mankind. Though PPI network research is considered extremely important in the field, there is an issue – we do not have enough people who have enough interdisciplinary knowledge in both the fields of biology and computer science; this limits our rate of progress in the field. Most biologists that are not expert coders need a way of calculating graph values and information that will help them analyze the graphs better without having to manipulate the data themselves. In this research, I test a few ways of achieving results through the use of available frameworks and algorithms, present the results and compare each method’s efficacy. My analysis takes place on very large datasets where I calculate several centralities and other data from the graph using different metrics, and I also visualize them in order to gain further insight. I also managed to note the significance of MPI and multithreading on the results thus obtained that suggest building scalable tools will help improve the analysis immensely.
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Johnson, David H. "High-throughput self-interaction chromatography applications in formulation prediction for proteins /." Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2009r/johnson.pdf.

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Thesis (M.S.)--University of Alabama at Birmingham, 2008.
Title from PDF title page (viewed Sept. 21, 2009). Additional advisors: Martha W. Bidez, W. Michael Carson, Richard A. Gray, W. William Wilson. Includes bibliographical references.
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Jiménez, García Brian. "Development and optimization of high-performance computational tools for protein-protein docking." Doctoral thesis, Universitat de Barcelona, 2016. http://hdl.handle.net/10803/398790.

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Computing has pushed a paradigm shift in many disciplines, including structural biology and chemistry. This change has been mainly driven by the increase in performance of computers, the capacity of dealing with huge amounts of experimental and analysis data and the development of new algorithms. Thanks to these advances, our understanding on the chemistry that supports life has increased and it is even more sophisticated that we had never imagined before. Proteins play a major role in nature and are often described as the factories of the cell as they are involved in virtually all important function in living organisms. Unfortunately, our understanding of the function of many proteins is still very poor due to the actual limitations in experimental techniques which, at the moment, they can not provide crystal structure for many protein complexes. The development of computational tools as protein-protein docking methods could help to fill this gap. In this thesis, we have presented a new protein-protein docking method, LightDock, which supports the use of different custom scoring functions and it includes anisotropic normal analysis to model backbone flexibility upon binding process. Second, several interesting web-based tools for the scientific community have been developed, including a web server for protein-protein docking, a web tool for the characterization of protein-protein interfaces and a web server for including SAXS experimental data for a better prediction of protein complexes. Moreover, the optimizations made in the pyDock protocol and the increase in th performance helped our group to score in the 5th position among more than 60 participants in the past two CAPRI editions. Finally, we have designed and compiled the Protein-Protein (version 5.0) and Protein-RNA (version 1.0) docking benchmarks, which are important resources for the community to test and to develop new methods against a reference set of curated cases.
Gràcies als recents avenços en computació, el nostre coneixement de la química que suporta la vida ha incrementat enormement i ens ha conduït a comprendre que la química de la vida és més sofisticada del que mai haguéssim pensat. Les proteïnes juguen un paper fonamental en aquesta química i són descrites habitualment com a les fàbriques de les cèl·lules. A més a més, les proteïnes estan involucrades en gairebé tots els processos fonamentals en els éssers vius. Malauradament, el nostre coneixement de la funció de moltes proteïnes és encara escaig degut a les limitacions actuals de molts mètodes experimentals, que encara no són capaços de proporcionar-nos estructures de cristall per a molts complexes proteïna-proteïna. El desenvolupament de tècniques i eines informàtiques d’acoblament proteïna-proteïna pot ésser crucial per a ajudar-nos a reduir aquest forat. En aquesta tesis, hem presentat un nou mètode computacional de predicció d’acoblament proteïna-proteïna, LightDock, que és capaç de fer servir diverses funcions energètiques definides per l’usuari i incloure un model de flexibilitat de la cadena principal mitjançant la anàlisis de modes normals. Segon, diverses eines d’interès per a la comunitat científica i basades en tecnologia web han sigut desenvolupades: un servidor web de predicció d’acoblament proteïna-proteïna, una eina online per a caracteritzar les interfícies d’acoblament proteïna-proteïna i una eina web per a incloure dades experimentals de tipus SAXS. A més a més, les optimitzacions fetes al protocol pyDock i la conseqüent millora en rendiment han propiciat que el nostre grup de recerca obtingués la cinquena posició entre més de 60 grups en les dues darreres avaluacions de l’experiment internacional CAPRI. Finalment, hem dissenyat i compilat els banc de proves d’acoblament proteïna-proteïna (versió 5) i proteïna-ARN (versió 1), molt importants per a la comunitat ja que permeten provar i desenvolupar nous mètodes i analitzar-ne el rendiment en aquest marc de referència comú.
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Alford, John Randolph. "Physical stability of a therapeutic protein in high protein concentration aqueous formulations." Connect to online resource, 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3273726.

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Books on the topic "High protein"

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Eckhardt, Linda West. The high protein cookbook. New York: Clarkson Potter, 2000.

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V, Clark Charles. The new high protein diet. London: Vermilion, 2002.

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Clark, Charles V. The new high protein diet. London: Vermilion, 2007.

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Bostjan, Kobe, Guss Mitchell, and Huber Thomas Dr, eds. Structural proteomics: High-throughput methods. Totowa, N.J: Humana, 2008.

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Skipper, Joy. The healthy protein kitchen. Bath: Love Food, 2016.

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Vincentelli, Renaud, ed. High-Throughput Protein Production and Purification. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9624-7.

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Doyle, Sharon A., ed. High Throughput Protein Expression and Purification. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-196-3.

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Crowley, J. Protein peas: Guidelines for high yields. [Dublin]: Teagasc, 1988.

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A, Doyle Sharon, ed. High throughput protein expression and purification: Methods and protocols. Totowa, N.J: Humana Press, 2009.

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Munschauer, Mathias. High-Resolution Profiling of Protein-RNA Interactions. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16253-9.

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Book chapters on the topic "High protein"

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Feldman, M., L. Avivi, A. A. Levy, M. Zaccai, Y. Avivi, and E. Millet. "High Protein Wheat." In Biotechnology in Agriculture and Forestry, 593–614. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-662-10933-5_33.

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Doyle, Sean P., Xiulei Mo, Kun Qian, Danielle N. Cicka, Qiankun Niu, and Haian Fu. "CHAPTER 3. High Throughput Screening Methods for PPI Inhibitor Discovery." In Protein–Protein Interaction Regulators, 49–86. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781788016544-00049.

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Fung, Jia Jun, Karla Blöcher-Juárez, and Anton Khmelinskii. "High-Throughput Analysis of Protein Turnover with Tandem Fluorescent Protein Timers." In Methods in Molecular Biology, 85–100. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1732-8_6.

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AbstractTandem fluorescent protein timers (tFTs) are versatile reporters of protein dynamics. A tFT consists of two fluorescent proteins with different maturation kinetics and provides a ratiometric readout of protein age, which can be exploited to follow intracellular trafficking, inheritance and turnover of tFT-tagged proteins. Here, we detail a protocol for high-throughput analysis of protein turnover with tFTs in yeast using fluorescence measurements of ordered colony arrays. We describe guidelines on optimization of experimental design with regard to the layout of colony arrays, growth conditions, and instrument choice. Combined with semi-automated genetic crossing using synthetic genetic array (SGA) methodology and high-throughput protein tagging with SWAp-Tag (SWAT) libraries, this approach can be used to compare protein turnover across the proteome and to identify regulators of protein turnover genome-wide.
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Holdgate, Geoffrey A., and Paul E. Hemsley. "Ligand Discovery: High-Throughput Binding: Fluorescence ()." In Protein-Ligand Interactions, 231–46. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1197-5_10.

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Wada, A. "Automated and High-Speed DNA Sequencing - Computer Technology Promotes Biological Advances." In Protein Structure and Protein Engineering, 116–22. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-74173-9_14.

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Gunn, John R. "Computational Protein Folding." In High Performance Computing Systems and Applications, 333–43. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5611-4_32.

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Kühlbrandt, Werner. "High-Resolution Electron Crystallography of Membrane Proteins." In Membrane Protein Structure, 206–23. New York, NY: Springer New York, 1994. http://dx.doi.org/10.1007/978-1-4614-7515-6_9.

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Nölting, Bengt. "High kinetic resolution of protein folding events." In Protein Folding Kinetics, 51–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-03966-3_5.

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Nölting, Bengt. "High structural resolution of transient protein conformations." In Protein Folding Kinetics, 95–123. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-03966-3_8.

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O’Connell, David J., Mikael Bauer, Sara Linse, and Dolores J. Cahill. "Probing Calmodulin Protein–Protein Interactions Using High-Content Protein Arrays." In Methods in Molecular Biology, 289–303. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-286-1_20.

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Conference papers on the topic "High protein"

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Tseng, Fan-Gang. "From High Performance Protein Micro Chip Toward Ultra High Sensitive Single Molecule Nano Array." In ASME 2009 7th International Conference on Nanochannels, Microchannels, and Minichannels. ASMEDC, 2009. http://dx.doi.org/10.1115/icnmm2009-82291.

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Protein microarrays have been employed to screen tens to thousands of proteins simultaneously for the observation of the biochemical activities in the protein-protein, protein-nucleic acid and small molecule interactions. This technology allows high throughput analysis and holds great potential for basic molecular biology research, disease marker identification, toxicological response profiling and pharmaceutical target screening. However, proteins easily malfunction in harsh environments so that they are hardly preserved before the application because of their complex and fragile structures. On the other hand, identify scarce amount of proteins less than fM range is very important and challenge for disease diagnosis at very early stage. As a result, the procedures for protein micro array formation are very important for preserving protein functionality to ensure useful protein assays, as well as the improvement of the detection sensitivity up to single molecule event but with high dynamic range for disease early detection. Therefore, this paper provides a novel view from the preparation of high efficient protein micro chip toward ultra high sensitive single protein nano array through the technology integration of BioMEMS and Bio-Nanotechnology.
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Munch, Katharina, Claire Berton-Carabin, Karin Schroen, and Simeon Stoyanov. "Plant protein-stabilized emulsions: Implications of protein and non-protein components for lipid oxidation." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zznf4565.

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The use of plant proteins to stabilize oil-in-water (O/W) emulsions has been an increasing trend lately. The complexity of the available plant protein ingredients, along with the proteins’ physicochemical properties, require advanced processing that typically leads to substantial concentrations of non-protein components in the final isolates or concentrates. It is known that those components, such as polyphenols, phytic acid or phospholipids, can have a strong influence on the oxidative stability of emulsions. Thus, to understand the oxidative stability of plant protein-stabilized emulsions, the influence of the non-protein components also needs to be considered. Many food emulsions, such as mayonnaise or infant formula, are stabilized by not only proteins, but also phospholipids. Such an interfacial protein-phospholipid combination can also be found in oleosomes, natural lipid droplets which show a high oxidative stability. This stability has been attributed to their interfacial architecture in which oleosins and phospholipids form a tight physical barrier against pro-oxidant species. However, while the antioxidant properties of proteins are widely reported, the contribution of phospholipids to lipid oxidation in plant protein-based emulsions remains underexplored. In this work, we investigated how mixed interfacial plant proteins and phospholipids may be rationally used to control the oxidative stability of O/W emulsions. The interfacial composition was modulated by varying the ratio between pea proteins and sunflower phosphatidylcholine (PC) while keeping the total concentration of pea proteins constant. Increasing the phospholipid-to-protein ratio led to a monotonic decrease in the concentration of proteins and an increase of phospholipids at the interface, while the oxidative stability of those O/W emulsions changed in a non-monotonic pattern. The results were put in perspective by embedding them in a context of reviewing the potential implications of typical components in plant protein ingredients on lipid oxidation.
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Cao, Yiping, and Mahesh Khot. "Food protein self-assembly towards high-performance functional materials." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/oyxx3948.

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Proteins not only determine the essential life activities of living organisms and the nutritional value of food products, but also are promising raw materials for designing functional materials, including in the fields of food science, environmental science, and nanomaterials. In the last decade, self-assembly of food proteins, particularly fibrillization, has attracted significant interest, as the assembled nanostructures are characterized by abundant b-sheet structures, large aspect ratio, and diverse surface functional groups. These features offer the possibility to overcome existing technological bottlenecks, and the rational utilization can yield high-performance materials. This talk will focus on two examples: protein gels and plastics. In the first example, a quantitative relationship was established between the microstructure of protein nanofibrils and the macroscopic mechanical properties of the resulting gels. This was successfully used to build protein gels with mechanical properties comparable to those of artificial meat. In the second example, protein-based plastics with high mechanical property and reduced hygroscopicity are developed by combining protein copolymerization and self-assembly. This provides a potential strategy for developing sustainable food packaging materials.
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Li, Yixun, Behzad Rezaei, Alioune Ngom, and Luis Rueda. "Prediction of high-throughput protein-protein interactions based on protein sequence information." In 2015 IEEE Conference on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2015. http://dx.doi.org/10.1109/cibcb.2015.7300310.

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Schoenrock, Andrew, Daniel Burnside, Houman Moteshareie, Alex Wong, Ashkan Golshani, Frank Dehne, and James R. Green. "Engineering inhibitory proteins with InSiPS: the in-silico protein synthesizer." In SC15: The International Conference for High Performance Computing, Networking, Storage and Analysis. New York, NY, USA: ACM, 2015. http://dx.doi.org/10.1145/2807591.2807630.

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Tirtom, Sena, and Aslı Akpınar. "Dairy Protein vs. Plant Protein and Their Consumer Perception." In 7th International Students Science Congress. Izmir International guest Students Association, 2023. http://dx.doi.org/10.52460/issc.2023.026.

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Proteins are crucial macronutrient for human health. Animal, dairy, and some plant proteins are considered high-quality proteins that provide health and metabolic benefits based on the digestible levels of essential amino acids they contain. Animal protein is rich in many essential amino acids, but excessive animal protein intake greatly increases fat intake. Therefore, due to the improvement in people's living standards and increase in protein intake, the animal protein supply is not sufficient to meet the increasing demand of people. Technologically, milk proteins are the most important component of milk due to their unique properties that allow milk to be converted into a wide range of products such as cheese or yoghurt quite easily. It is widely accepted that dairy products are excellent sources of highly digestible essential amino acids. Nowadays, plant protein is preferred because has advantages such as it is an abundant source, cheap, easy to obtain, preferred by special consumer groups such as vegan/vegetarian, does not contain cholesterol and preventing diseases. In the last decades, the increasing interest of both producers and consumers in plant proteins and the decrease in animal protein intake and inclination to plant protein intake with the innovations in the markets emphasize the importance of these alternative sources. In this review, information is given about the importance of milk proteins and plant proteins and the role they play in consumer preference is mentioned.
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Walker, F. J. "REGULATION OF THE ANTICOAGULANT ACTIVITY OF ACTIVATED PROTEIN C BY PROTEIN S AND PROTEIN S BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642964.

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Protein S is a vitamin K-dependent protein that acts as a cofactor for the anticoagulant activity of activated protein C both in the proteolytic inactivation of factor V and VIII. Protein S is a single chain protein with a molecular weight of approximately 62 kDa. When the molecular weight of protein S in plasma was determined it was found to be much larger than the single chain protein. The molecular weight of functional protein S when measured by sedimentation equilibrium with the air-driven ultracentrifuge was observed to be between 115 and 130 kDa. In high salt or in the presence of copper ions this was observed to be reduced to approximately 62 kDa. Frontal analysis of plasma indicated that the functional protein by exist in as many as three molecular weight foras. Gel filtration of radiolabeled protein S also indicates heterogeneity in the molecular weight. In order to isolate the binding protein, bovine plasma was fractionated first on a column of immobilized iminodiacetic acid that had been equilibrated with copper ions. The proteins that eluted in the 0.6 M NaCl wash were passed over a column of protein S immobilized on agarose beads. A single protein was observed to elute from the protein S agarose at high salt. Fractionation of human plasma indicated the presence of several proteins. One major component isolated was C4-binding protein. A second major component has also been isolated that appears to correspond to protein S-binding protein that has been isolated from bovine plasma. When added to plasma depleted of both protein S and the binding protein, the binding protein was observed to enhance the anticoagulant activity of activated protein C only in the presence of protein S. Protein S-binding protein was also observed to enhance the rate of factor Va inactivation by activated protein C and protein S.
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Загороднюк, Л. Х., L. H. Zagorodnyuk, Д. С. Махортов, D. S. Mahortov, А. С. Чепенко, A. S. Chepenko, И. Н. Туцкая, I. N. Tuckaya, Н. А. Науменко, and N. A. Naumenko. "PLASTICIZERS BASED ON ANIMAL PROTEIN PROTEIN." In International Scientific and Practical 65th anniversary conference BSTU them. V.G. Shukhov "HIGH-TECH TECHNOLOGIES AND INNOVATIONS (XXIII scientific readings)". Belgorod State Technological University named after V.G. Shukhov, 2019. http://dx.doi.org/10.12737/conferencearticle_5cecedc24d0f67.83326643.

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KÖhlin, A., and J. Stenflo. "HIGH AFFINITY CALCIUM BINDING TO DOMAINES OF PROTEIN C THAT ARE HOMOLOGUS TO THE EPIDERMAL GROWTH FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643645.

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In addition to γ-carboxyglutamic acid (Gla)-dependent calcium binding all of the vitamin K-dependent plasma proteins, except prothrombin, have one or two high affinity calcium binding sites that do not require the Gla residues. A common denominator among these proteins (factors IX, X, protein C, protein Z and protein S) is that they have domaines that are homologus to the epidermal growth factor (EGF) precursor. In factors VII,IX,X, protein C and in protein Z the aminoterminal of two EGF homology regions contain one residue of β-hydroxyaspartic acid (Hya) whereas in protein S the aminoterminal EGF homology region contains Hya and the three following contain one β-hydroxyasparagine residue each.In an attempt to elucidate the role of the EGF homology regions in the Gla independent calcium binding we have isolated a tryptic fragment (residue 44-138) from the light chain of human protein C. The fragment was isolated using a monoclonal antibody that recognizes a calcium ion stabilized epitope that is expressed both in intact protein C and in protein C lacking the Gla domaine.The antibody bound the isolated EGF homology region in the presence of calcium ions but not in EDTA containing buffer. A calcium ion titration showed half maximal binding at approximately 200 μM Ca2+. The metal ion induced conformational change in the isolated fragment was also studied with affinity purified rabbit antibodies against Gla domainless protein C. Antibodies that bound in the presence of calcium ions and that could be eluted with EDTA recognized the metal ion induced conformational change in the isolated EGF homology domain. Our results suggest that one or both of the EGF homology regions are involved in the Gla-independent high affinity calcium binding in the vitamin K-dependent plasma proteins.
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Munro, Troy, Changhu Xing, Heng Ban, Cameron Copeland, and Randolph Lewis. "Probing the Mysteries of Spider Silk’s Uncharacteristically High Thermal Diffusivity." In ASME 2013 Heat Transfer Summer Conference collocated with the ASME 2013 7th International Conference on Energy Sustainability and the ASME 2013 11th International Conference on Fuel Cell Science, Engineering and Technology. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/ht2013-17493.

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Spider silks exhibit excellent strength, stiffness, and toughness simultaneously, a feat unachievable in most synthetic, structural materials. It has recently been reported that the thermal conductivity of dragline silk is comparable to copper, which is uncharacteristically high for a biomaterial. In order to develop a fundamental understanding of the high thermal properties of spider silk, further research must be made to explore how the structure and organization of spider silk proteins affects heat transfer characteristics. Synthetically produced silks created from spider silk proteins obtained from transgenic sources can be used to determine these protein structure effects by varying protein content and process treatments. This initial study determined the thermal properties of synthetic spider silk created from transgenic goat’s milk proteins using the transient electrothermal method (TET). Results show that the thermal properties of the synthetic silk are lower than the natural spider silk but vary based on the process treatment, and that the annealing of the gold film coated on the fiber has no effect on the measured thermal properties. These results provide a framework for further research on the protein content effect and its role in thermal properties.
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Reports on the topic "High protein"

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Li, Fenglei. Automated High Throughput Protein Crystallization Screening at Nanoliter Scale and Protein Structural Study on Lactate Dehydrogenase. Office of Scientific and Technical Information (OSTI), August 2006. http://dx.doi.org/10.2172/892735.

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Handakumbura, Pubudu, Aaron Ogden, Amirhossein Ahkami, and Mowei Zhou. High-throughput screening of Protein-DNA interactions in Sorghum. Office of Scientific and Technical Information (OSTI), September 2020. http://dx.doi.org/10.2172/2331467.

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Chamovitz, Daniel A., and Zhenbiao Yang. Chemical Genetics of the COP9 Signalosome: Identification of Novel Regulators of Plant Development. United States Department of Agriculture, January 2011. http://dx.doi.org/10.32747/2011.7699844.bard.

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This was an exploratory one-year study to identify chemical regulators of the COP9 signalosome. Chemical Genetics uses small molecules to modify or disrupt the function of specific genes/proteins. This is in contrast to classical genetics, in which mutations disrupt the function of genes. The underlying concept is that the functions of most proteins can be altered by the binding of a chemical, which can be found by screening large libraries for compounds that specifically affect a biological, molecular or biochemical process. In addition to screens for chemicals which inhibit specific biological processes, chemical genetics can also be employed to find inhibitors of specific protein-protein interactions. Small molecules altering protein-protein interactions are valuable tools in probing protein-protein interactions. In this project, we aimed to identify chemicals that disrupt the COP9 signalosome. The CSN is an evolutionarily conserved eight-subunit protein complex whose most studied role is regulation of E3 ubiquitinligase activity. Mutants in subunits of the CSN undergo photomorphogenesis in darkness and accumulate high levels of pigments in both dark- and light-grown seedlings, and are defective in a wide range of important developmental and environmental-response pathways. Our working hypothesis was that specific molecules will interact with the CSN7 protein such that binding to its various interacting proteins will be inhibited. Such a molecule would inhibit either CSN assembly, or binding of CSN-interacting proteins, and thus specifically inhibit CSN function. We used an advanced chemical genetic screen for small-molecule-inhibitors of CSN7 protein-protein interactions. In our pilot study, following the screening of ~1200 unique compounds, we isolated four chemicals which reproducibly interfere with CSN7 binding to either CSN8 or CSN6.
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Brice, Jeremy. Investment, power and protein in sub-Saharan Africa. Edited by Tara Garnett. TABLE, October 2022. http://dx.doi.org/10.56661/d8817170.

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The place of protein in sub-Saharan Africa’s food system is changing rapidly, raising complex international development, global health and environmental sustainability issues. Despite substantial growth in the region’s livestock agriculture sector, protein consumption per capita remains low, and high levels of undernourishment persist. Meanwhile sub-Saharan Africa’s population is growing and urbanising rapidly, creating expectations that demand for protein will increase rapidly over the coming decades and triggering calls for further investment in the expansion and intensification of the region’s meat and dairy sector. However, growing disquiet over the environmental impacts of further expansion in livestock numbers, and growing sales of alternative protein products in the Global North, has raised questions about the future place of plant-based, insect and lab-grown proteins in African diets and food systems. This report examines financial investment in protein production in sub-Saharan Africa. It begins from the position that investors play an important role in shaping the development of diets and food systems because they are able to mobilise the financial resources required to develop new protein products, infrastructures and value chains, or to prevent their development by withholding investment. It therefore investigates which actors are financing the production in sub-Saharan Africa of: a) animal proteins such as meat, fish, eggs and dairy products; b) ‘protein crops’ such as beans, pulses and legumes; and c) processed ‘alternative proteins’ derived from plants, insects, microbes or animal cells grown in a tissue culture. Through analysing investment by state, philanthropic and private sector organisations – as well as multilateral financial institutions such as development banks – it aims to establish which protein sources and stages of the value chain are financed by different groups of investors and to explore the values and goals which shape their investment decisions. To this end, the report examines four questions: 1. Who is currently investing in protein production in sub-Saharan Africa? 2. What goals do these investors aim to achieve (or what sort of future do they seek to bring about) through making these investments? 3. Which protein sources and protein production systems do they finance? 4. What theory of change links their investment strategy to these goals? In addressing these questions, this report explores what sorts of protein production and provisioning systems different investor groups might be helping to bring into being in sub-Saharan Africa. It also considers what alternative possibilities might be marginalised due to a lack of investment. It thus seeks to understand whose priorities, preferences and visions for the future of food might be informing the changing place of protein in the region’s diets, economies and food systems.
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Hermann, J. R., and Mark S. Honeyman. Okara: A Possible High Protein Feedstuff For Organic Pig Diets. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-197.

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Fries, Krysten, and Elizabeth Bobeck. Energy Digestibility of a High Protein DDGS Product in Broilers. Ames (Iowa): Iowa State University, January 2018. http://dx.doi.org/10.31274/ans_air-180814-349.

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Fries, Krysten, and Elizabeth Bobeck. Evaluation of a High Protein DDGS Product on Broiler Performance. Ames (Iowa): Iowa State University, January 2018. http://dx.doi.org/10.31274/ans_air-180814-402.

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Fries, Krysten, and Elizabeth Bobeck. Amino Acid Digestibility of a High Protein DDGS Product in Broilers. Ames (Iowa): Iowa State University, January 2018. http://dx.doi.org/10.31274/ans_air-180814-336.

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Varga, Gabriella A., Amichai Arieli, Lawrence D. Muller, Haim Tagari, Israel Bruckental, and Yair Aharoni. Effect of Rumen Available Protein, Amimo Acids and Carbohydrates on Microbial Protein Synthesis, Amino Acid Flow and Performance of High Yielding Cows. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568103.bard.

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The effect of rumen available protein amino acids and carbohydrates on microbial protein synthesis, amino acid flow and performance of high yielding dairy cows was studied. A significant relationship between the effective degradabilities of OM in feedstuffs and the in vivo ruminal OM degradation of diets of dairy cows was found. The in situ method enabled the prediction of ruminal nutrients degradability response to processing of energy and nitragenous supplements. The AA profile of the rumen undegradable protein was modified by the processing method. In a continuous culture study total N and postruminal AA flows, and bacterial efficiency, is maximal at rumen degradable levels of 65% of the CP. Responses to rumen degradable non carbohydrate (NSC) were linear up to at least 27% of DM. Higher CP flow in the abomasum was found for cows fed high ruminally degradable OM and low ruminally degradable CP diet. It appeared that in dairy cows diets, the ratio of rumen degradable OM to rumenally degradable CP should be at least 5:1 in order to maximize postruminal CP flow. The efficiency of microbial CP synthesis was higher for diets supplemented with 33% of rumen undegradable protein, with greater amounts of bacterial AA reaching the abomasum. Increase in ruminal carbohydrate availability by using high moisture corn increased proportions of propionate, postruminal nutrients flow, postruminal starch digestibility, ruminal availability of NSC, uptake of energy substrates by the mammory gland. These modifications resulted with improvement in the utilization of nonessential AA for milk protein synthesis, in higher milk protein yield. Higher postruminal NSC digestibility and higher efficiency of milk protein production were recorded in cows fed extruded corn. Increasing feeding frequency increased flow of N from the rumen to the blood, reduced diurnal variation in ruminal and ammonia, and of plasma urea and improved postruminal NSC and CIP digestibility and total tract digestibilities. Milk and constituent yield increased with more frequent feeding. In a study performed in a commercial dairy herd, changes in energy and nitrogenous substrates level suggested that increasing feeding frequency may improve dietary nitrogen utilization and may shift metabolism toward more glucogenesis. It was concluded that efficiency of milk protein yield in high producing cows might be improved by an optimization of ruminal and post-ruminal supplies of energy and nitrogenous substrates. Such an optimization can be achieved by processing of energy and nitrogenous feedstuffs, and by increasing feeding frequency. In situ data may provide means for elucidation of the optimal processing conditions.
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Stender, David, Colin Johnson, Don Hummel, and Wayne Roush. Decrease in Protein Level in Final Finishing Phase of High Lean Gain Swine. Ames (Iowa): Iowa State University, January 2007. http://dx.doi.org/10.31274/ans_air-180814-707.

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