Gotowe bibliografie tematyczne / Protein conformation

Spis treści

  1. Artykuły w czasopismach
  2. Rozprawy doktorskie
  3. Książki
  4. Części książek
  5. Streszczenia konferencji
  6. Raporty organizacyjne

Gotowa bibliografia na temat „Protein conformation”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 25 lipca 2025

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Artykuły w czasopismach na temat "Protein conformation"

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Cresti, Julianna R., Abramo J. Manfredonia, Christopher E. Bragança, et al. "Proteasomal conformation controls unfolding ability." Proceedings of the National Academy of Sciences 118, no. 25 (2021): e2101004118. http://dx.doi.org/10.1073/pnas.2101004118.

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The 26S proteasome is the macromolecular machine responsible for the bulk of protein degradation in eukaryotic cells. As it degrades a ubiquitinated protein, the proteasome transitions from a substrate-accepting conformation (s1) to a set of substrate-processing conformations (s3 like), each stabilized by different intramolecular contacts. Tools to study these conformational changes remain limited, and although several interactions have been proposed to be important for stabilizing the proteasome’s various conformations, it has been difficult to test these directly under equilibrium conditions
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Ohhashi, Yumiko, Yoshiki Yamaguchi, Hiroshi Kurahashi, et al. "Molecular basis for diversification of yeast prion strain conformation." Proceedings of the National Academy of Sciences 115, no. 10 (2018): 2389–94. http://dx.doi.org/10.1073/pnas.1715483115.

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Self-propagating β-sheet–rich fibrillar protein aggregates, amyloid fibers, are often associated with cellular dysfunction and disease. Distinct amyloid conformations dictate different physiological consequences, such as cellular toxicity. However, the origin of the diversity of amyloid conformation remains unknown. Here, we suggest that altered conformational equilibrium in natively disordered monomeric proteins leads to the adaptation of alternate amyloid conformations that have different phenotypic effects. We performed a comprehensive high-resolution structural analysis of Sup35NM, an N-te
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Cretin, Gabriel, Tatiana Galochkina, Alexandre G. de Brevern, and Jean-Christophe Gelly. "PYTHIA: Deep Learning Approach for Local Protein Conformation Prediction." International Journal of Molecular Sciences 22, no. 16 (2021): 8831. http://dx.doi.org/10.3390/ijms22168831.

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Protein Blocks (PBs) are a widely used structural alphabet describing local protein backbone conformation in terms of 16 possible conformational states, adopted by five consecutive amino acids. The representation of complex protein 3D structures as 1D PB sequences was previously successfully applied to protein structure alignment and protein structure prediction. In the current study, we present a new model, PYTHIA (predicting any conformation at high accuracy), for the prediction of the protein local conformations in terms of PBs directly from the amino acid sequence. PYTHIA is based on a dee
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Seo, Udeok, Ku-Jin Kim, and Beom Kang. "An Algorithm for Computing Side Chain Conformational Variations of a Protein Tunnel/Channel." Molecules 23, no. 10 (2018): 2459. http://dx.doi.org/10.3390/molecules23102459.

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In this paper, a novel method to compute side chain conformational variations for a protein molecule tunnel (or channel) is proposed. From the conformational variations, we compute the flexibly deformed shapes of the initial tunnel, and present a way to compute the maximum size of the ligand that can pass through the deformed tunnel. By using the two types of graphs corresponding to amino acids and their side chain rotamers, the suggested algorithm classifies amino acids and rotamers which possibly have collisions. Based on the divide and conquer technique, local side chain conformations are c
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Merski, Matthew, Marcus Fischer, Trent E. Balius, Oliv Eidam, and Brian K. Shoichet. "Homologous ligands accommodated by discrete conformations of a buried cavity." Proceedings of the National Academy of Sciences 112, no. 16 (2015): 5039–44. http://dx.doi.org/10.1073/pnas.1500806112.

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Conformational change in protein–ligand complexes is widely modeled, but the protein accommodation expected on binding a congeneric series of ligands has received less attention. Given their use in medicinal chemistry, there are surprisingly few substantial series of congeneric ligand complexes in the Protein Data Bank (PDB). Here we determine the structures of eight alkyl benzenes, in single-methylene increases from benzene to n-hexylbenzene, bound to an enclosed cavity in T4 lysozyme. The volume of the apo cavity suffices to accommodate benzene but, even with toluene, larger cavity conformat
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DOWNING, Donald T., та N. D. LAZO. "Molecular modelling indicates that the pathological conformations of prion proteins might be β-helical". Biochemical Journal 343, № 2 (1999): 453–60. http://dx.doi.org/10.1042/bj3430453.

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Creutzfeldt-Jakob disease, kuru, scrapie and bovine spongiform encephalopathy are diseases of the mammalian central nervous system that involve the conversion of a cellular protein into an insoluble extracellular isoform. Spectroscopic studies have shown that the precursor protein contains mainly α-helical and random-coil conformations, whereas the prion isoform is largely in the β conformation. The pathogenic prion is resistant to denaturation and protease digestion and can promote the conversion of the precursor protein to the pathogenic form. These properties have yet to be explained in ter
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Avdeev, P. A., V. A. Ignatenko, Yu V. Kornoushenko, and L. A. Evtuhova. "EFFECT OF DIFFERENT CONCENTRATIONS OF UREA AND PH ON THE FLUORESCENCE PARAMETERS OF BOVINE SERUM ALBUMIN." Health and Ecology Issues, no. 1 (March 28, 2011): 106–10. http://dx.doi.org/10.51523/2708-6011.2011-8-1-20.

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Urea is a chemical effect on the conformation of bovine serum albumin, causing a partial unfolding of the protein globule its exit to the surface of hydrophobic amino acids. Changing the pH of the solution in which the protein also affects the state of the protein, so there are multiple conformational states in which urea as a chemical effect on the conformation of bovine serum albumin, causing a partial unfolding of the protein globule of its exit to the surface of hydrophobic amino acids. Changing the pH of the solution in which the protein also affects the state of the protein, so there are
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Giri Rao, V. V. Hemanth, and Shachi Gosavi. "On the folding of a structurally complex protein to its metastable active state." Proceedings of the National Academy of Sciences 115, no. 9 (2018): 1998–2003. http://dx.doi.org/10.1073/pnas.1708173115.

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For successful protease inhibition, the reactive center loop (RCL) of the two-domain serine protease inhibitor, α1-antitrypsin (α1-AT), needs to remain exposed in a metastable active conformation. The α1-AT RCL is sequestered in a β-sheet in the stable latent conformation. Thus, to be functional, α1-AT must always fold to a metastable conformation while avoiding folding to a stable conformation. We explore the structural basis of this choice using folding simulations of coarse-grained structure-based models of the two α1-AT conformations. Our simulations capture the key features of folding exp
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Mizutani, Tadashi, and Shigeyuki Yagi. "Linear tetrapyrroles as functional pigments in chemistry and biology." Journal of Porphyrins and Phthalocyanines 08, no. 03 (2004): 226–37. http://dx.doi.org/10.1142/s1088424604000210.

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1,19,21,24-tetrahydro-1,19-bilindione is the framework of pigments frequently found in nature, which includes biliverdin IX α, phytochromobilin and phycocyanobilin. 1,19-bilindiones have unique features such as (1) photochemical and thermal cis-trans isomerization, (2) excited energy transfer, (3) chiroptical properties due to the cyclic helical conformation, (4) redox activity, (5) coordination to various metals, and (6) reconstitution to proteins. 1,19-bilindione can adopt a number of conformations since it has exocyclic three double bonds and three single bonds that are rotatable thermally
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Egorov, Vladimir, Natalia Grudinina, Andrey Vasin, and Dmitry Lebedev. "Peptide-Induced Amyloid-Like Conformational Transitions in Proteins." International Journal of Peptides 2015 (September 8, 2015): 1–5. http://dx.doi.org/10.1155/2015/723186.

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Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can c
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Rozprawy doktorskie na temat "Protein conformation"

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Link, Justin J. "Ultrafast Protein Conformation Dynamics." The Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=osu1230584570.

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Wang, Chu. "Improved conformational sampling for protein-protein docking /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/9194.

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Billsten, Peter. "Studies on the conformation of adsorbed proteins." Lund : Göteborg University, 1997. http://catalog.hathitrust.org/api/volumes/oclc/39776983.html.

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Florane, H. "Exploring protein conformation with mass spectrometry." Thesis, University of Edinburgh, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.650980.

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The first part of this thesis describes the development and viability of a phase I screening system for obtaining a rank order of affinity of novel ligands against the immunophilin, Cyclophilin A (CypA). The naturally occurring inhibitor Cyclosporin A (CsA) was used as a positive control to validate a method for calculating the dissociation constant (K<sub>d</sub>). An HPLC autosampler and pumping system was used as a high throughput on-line electrospray ionisation (ESI)-MS sampling system. Optimised ESI conditions were then used to screen novel ligands from 3 combinatorial libraries and appro
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Nicholls, Robert Adam. "Conformation-independent comparison of protein structures." Thesis, University of York, 2011. http://etheses.whiterose.ac.uk/2120/.

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The comparative analysis of protein structures is often performed in order to identify and explore similarities/dissimilarities present between target structures. Whilst many tools are available for structural comparison, the development of new tools providing different information is desirable. The work presented here concerns the development of ProSMART (Procrustes Structural Matching Alignment and Restraints Tool), a tool to aid the comparative analysis of protein structures. Primarily, the software is used for conformation-independent pairwise structural alignment, allowing identification
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Watt, Stephen J. "Use of electrospray ionization mass spectrometry to study protein conformation and protein-protein interactions." Access electronically, 2005. http://www.library.uow.edu.au/adt-NWU/public/adt-NWU20060516.114814/index.html.

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Thesis (Ph.D.)--University of Wollongong, 2005.<br>Typescript. EMBARGOED-this thesis is subject to a six months embargo (07/09/06) and may only be viewed and copied with the permission of the author. For further information please Contact the Archivist. Includes bibliographical references: leaf 159-194.
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Rashid, Mahmood Abdur. "Heuristic Based Search for Protein Structure Prediction." Thesis, Griffith University, 2014. http://hdl.handle.net/10072/367134.

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Proteins that are essentially sequences of amino acids, adopt specific folded 3-dimensional (3D) structures to perform their specific tasks. However, misfolded proteins cause fatal diseases. Hence, protein structure prediction (PSP) has emerged as an important multi-disciplinary research problem. Given a protein sequence, the PSP problem is to find a 3D structure of the protein such that the total free energy amongst the amino acids in the sequence is minimised. In-vitro laboratory methods are time-consuming, expensive, and failure-prone. Conversely, computational methods are NP-hard even when
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Chivian, Dylan Casey. "Application of information from homologous proteins for the prediction of protein structure /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/9264.

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Hosia, Waltteri. "Molecular mechanisms in amyloid fibril formation /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7349-976-5.

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Sandin, Sara. "Cryo-electron tomography of individual protein molecules /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-462-7/.

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Książki na temat "Protein conformation"

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Symposium on Protein Conformation (1991 : Ciba Foundation), ed. Protein conformation. Wiley, 1991.

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Hamaguchi, Kōzō. The protein molecule: Conformation, stability, and folding. Japan Scientific Societies Press, 1992.

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A, Shirley Bret, ed. Protein stability and folding: Theory and practice. Humana Press, 1995.

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B, Roswell Linda, ed. Protein conformation: New research. Nova Science Publishers, 2008.

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E, Sternberg Michael J., ed. Protein structure prediction: A practical approach. IRL Press at Oxford University Press, 1996.

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Joël, Janin, and Wodak Shoshana J, eds. Protein modules and protein-protein interaction. Academic Press, 2002.

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Siddhartha, Roy, and Biswas B. B, eds. Subcellular biochemistry. Plenum, 1995.

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D, Fasman Gerald, ed. Prediction of protein structure and the principles of protein confirmation. Plenum, 1989.

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D, Fasman Gerald, ed. Prediction of protein structure and the principles of protein conformation. Plenum Press, 1989.

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P, Creamer Trevor, ed. Unfolded proteins: From denatured to intrinsically disordered. Nova Science, 2008.

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Części książek na temat "Protein conformation"

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Jaenicke, Rainer. "Protein Stability and Protein Folding." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch13.

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Alber, Tom. "Stabilization Energies of Protein Conformation." In Prediction of Protein Structure and the Principles of Protein Conformation. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1571-1_5.

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Duquerroy, Stéphane, Jacqueline Cherfils, and Joël Janin. "Protein-Protein Interaction: An Analysis by Computer Simulation." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch15.

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Na, Hyuntae, and Guang Song. "Ellipsoid-Weighted Protein Conformation Alignment." In Bioinformatics Research and Applications. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-38036-5_27.

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Richardson, Jane S., and David C. Richardson. "Principles and Patterns of Protein Conformation." In Prediction of Protein Structure and the Principles of Protein Conformation. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1571-1_1.

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Taneva, Stefka G., Sonia Bañuelos, and Arturo Muga. "Protein-membrane interaction: Lipid environment modulates protein conformation." In Spectroscopy of Biological Molecules: New Directions. Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4479-7_152.

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Baldwin, Robert L. "Experimental Studies of Pathways of Protein Folding." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch12.

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Richards, F. M. "Introduction." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch1.

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Gunsteren, W. F. van, P. Gros, A. E. Torda, H. J. C. Berendsent, and R. C. van Schaik. "On Deriving Spatial Protein Structure from NMR or X-Ray Diffraction Data." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch10.

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Dobson, Christopher M. "NMR Spectroscopy and Protein Folding: Studies of Lysozyme and α-Lactalbumin." In Ciba Foundation Symposium 161 - Protein Conformation. John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514146.ch11.

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Streszczenia konferencji na temat "Protein conformation"

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Lonika, Charistika, Dono Indarto, and Amelya Augusthina Ayusari. "Roseoside from Lemon Fruits (<i>Citrus limon)</i> as a Potential Inhibitor of Cluster of Differentiation 36 for Obesity Treatment." In 8th International Conference on Advanced Material for Better Future. Trans Tech Publications Ltd, 2025. https://doi.org/10.4028/p-vo3mlu.

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Obesity is a global health problem that prevalence has increased in the last decade. Triglycerides are the main fat component in daily food intake, which can be absorbed directly into the enterocytes through Cluster of Differentiation (CD) 36 transporter protein. Glucagon-like peptide 1 receptor agonist (semaglutide) has recently been approved for obesity treatment, but this medicine has some side effects in the gastrointestinal tract. Administration of Lactobacillus-fermented lemon juice reduced serum triglyceride levels and body weight (BW) of obese rats but it is not related to the action o
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Xu, Yangqing, and Gang Bao. "Protein Conformational Changes Under Applied Forces." In ASME 1999 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1999. http://dx.doi.org/10.1115/imece1999-0408.

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Abstract Recent studies confirm that stresses, including that due to gravity, tension, compression, pressure, and shear influence cell growth, differentiation, secretion, movement, signal transduction, and gene expression. Yet, little is known about how cells sense the mechanical stresses or deformations, and convert these mechanical signals into biological or biochemical responses. A possible mechno-chemical coupling mechanism involves protein conformational changes under mechanical forces. Our hypothesis is that mechanical forces can cause large changes of the conformation of proteins, which
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Karplus, M. "Internal dynamics of macromolecules : Simulations of motion in proteins." In International Conference on Ultrafast Phenomena. Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.thb1.

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The internal motions of proteins will be discussed. Detailed atom-bases simulations of the native conformation space will be supplemented by simplified models for the full conformation space involved in protein folding.
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Škrhák, Vít, and David Hoksza. "Framework for Protein Structures Conformation Analysis." In 2023 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2023. http://dx.doi.org/10.1109/bibm58861.2023.10385905.

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Kazerounian, Kazem, Khalid Latif, Kimberly Rodriguez, and Carlos Alvarado. "ProtoFold: Part I — Nanokinematics for Analysis of Protein Molecules." In ASME 2004 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/detc2004-57243.

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Proteins are evolution’s mechanisms of choice. Study of nano-mechanical systems must encompass an understanding of the geometry and conformation of protein molecules. Proteins are open or closed loop kinematic chains of miniature rigid bodies connected by revolute joints. The Kinematics community is in a unique position to extend the boundaries of knowledge in nano biomechanical systems. ProtoFold is a software package that implements novel and comprehensive methodologies for ab initio prediction of the final three-dimensional conformation of a protein, given only its linear structure. In this
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Kumar, Sugam, I. Yadav, V. K. Aswal, and J. Kohlbrecher. "Modifications in nanoparticle-protein interactions by varying the protein conformation." In DAE SOLID STATE PHYSICS SYMPOSIUM 2016. Author(s), 2017. http://dx.doi.org/10.1063/1.4980309.

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Koh, Sung K., and G. K. Ananthasuresh. "Design of HP Models of Proteins by Energy Gap Criterion Using Continuous Modeling and Optimization." In ASME 2004 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/detc2004-57598.

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The sequence of 20 types of amino acid residues in a heteropolymer chain of a protein is believed to be the basis for the 3-D conformation (folded structure) that a protein assumes to serve its functions. We present a deterministic optimization method to design the sequence of a simplified model of proteins for a desired conformation. A design methodology developed for the topology optimization of compliant mechanisms is adapted here by converting the discrete combinatorial problem of protein sequence design to a continuous optimization problem. It builds upon our recent work which used a mini
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Poort, S. R., C. Krommenhoek-van Es, I. K. van der Linden, N. H. van Tilburg, and R. M. Bertina. "DEFECTS OF VITAMIN K-DEPENDENT FACTORS IN CA(11)-STABILI ZED STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644320.

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Vitamin K-dependent (anti)coagulation factors (factor II, VII, IX, X protein C and S) undergo a conformational transition upon binding of Ca(II), which is a prerequisite for their normal function. Abnormalities in these properties occur during vitamin K deficiency or treatment with anti vitamin K drugs and in some genetic variants of coagulation factors. Immunological assays utilizing antibodies against the Ca(II)-stabilized structure are useful to detect such abnormalities.Starting from specific rabbit antisera antibody populations specific for the Ca(II)-dependent conformation of factor II,
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Buzdalov, Maxim, Sergey Knyazev, and Yury Porozov. "Protein Conformation Motion Modeling Using Sep-CMA-ES." In 2014 13th International Conference on Machine Learning and Applications (ICMLA). IEEE, 2014. http://dx.doi.org/10.1109/icmla.2014.12.

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Sapin, Emmanuel, Kenneth De Jong, and Amarda Shehu. "Evolving Conformation Paths to Model Protein Structural Transitions." In BCB '17: 8th ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics. ACM, 2017. http://dx.doi.org/10.1145/3107411.3107498.

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Raporty organizacyjne na temat "Protein conformation"

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Zhu, Xiaoyang. Controlling Protein Conformation and Activities on Block-Copolymer Nanopatterns. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada607976.

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Zhu, Xiaoyang, and Tim P. Lodge. Controlling Protein Conformation & Activities on Block-Copolymer Nanopatterns. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada520626.

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Hanke, Andreas. Studies of Single Biomolecules, DNA Conformational Dynamics, and Protein Binding. Defense Technical Information Center, 2008. http://dx.doi.org/10.21236/ada483440.

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Lu, Hong P. Controlling Protein Conformations to Explore Unprecedented Material Properties by Single-Molecule Surgery. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada584676.

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Schubert, David R., Yuanbin Liu, and Roland Riek. The Antemortem Detection and Conformational Switches of Prion Proteins. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada446422.

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Beck, Thomas, Nimal Wijesekera, David Rogers, and Roman Petrenko. Multiscale Modeling of Complex Systems Conformational Transitions in Proteins. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada482296.

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McGuirl, Michele A. Elucidation of Prion Protein Conformational Changes Associated With Infectivity by Fluorescence Spectroscopy. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada426340.

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McGuirl, Michele A., and Jessica Gilbert. Elucidation of Prion Protein Conformational Changes Associated with Infectivity by Fluorescence Spectroscopy. Defense Technical Information Center, 2007. http://dx.doi.org/10.21236/ada575958.

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McGuirl, Michele. Elucidation of Prion Protein Conformational Changes Associated with Infectivity by Fluorescence Spectroscopy. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada462868.

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Kim, Sangtae. Microstructural Models of Interactions That Govern Protein Conformations: Algorithms for High Performance Computer Architectures. Defense Technical Information Center, 1998. http://dx.doi.org/10.21236/ada360981.

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