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Relevant bibliographies by topics / Amino acids - Structure

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Academic literature on the topic 'Amino acids - Structure'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "Amino acids - Structure"

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Athmani, Hamza, and Nourreedine Benali-Cherif. "Structure and thermal analysis of amino acids." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C989. http://dx.doi.org/10.1107/s205327331409010x.

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The twenty amino acids are chemical compounds having two functional groups (carboxyl:-COOH, amine:-NH2) and an asymmetric carbon (except glycine). They are amphoteric and can exist as zwitterion. Because of the reactivity of amino acids (esterification, amidation, N-alkylisation, N-arylation, protonation), and their conformation (aliphatic, aromatic) chemical, properties (acid, base, and / or hydroxylated, solubility), and physical properties (absorbance, NLO), our laboratory contribute to the study (synthesis and X ray single crystal structures) of new organic-inorganic hybrid compounds which

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RAWLS, REBECCA. "Chiral Amino Acids Alter Mineral Structure." Chemical & Engineering News 79, no. 25 (2001): 11. http://dx.doi.org/10.1021/cen-v079n025.p011a.

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Nikiforov, L. A., M. V. Belousov, and N. S. Fursa. "Study of amino-acid structure Lemna minor L." Bulletin of Siberian Medicine 10, no. 5 (2011): 74–77. http://dx.doi.org/10.20538/1682-0363-2011-5-74-77.

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For the first time qualitative and quantitative amino-acid structure Lemna minor L. is studied with use of a highly effective liquid chromatography. Presence 18 proteinogennic amino acids, including 8 irreplaceable is established. The sum of replaceable amino acids of a duckweed small is presented monoaminocarboxylic,monoaminodicarboxylic, diaminomonocarboxylic and heterocyclic acids. Irreplaceable amino acids are presented monoaminomonocarboxylic and diaminomonocarboxylic by acids.

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Koehl, P., and M. Levitt. "Structure-based conformational preferences of amino acids." Proceedings of the National Academy of Sciences 96, no. 22 (1999): 12524–29. http://dx.doi.org/10.1073/pnas.96.22.12524.

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Tsai, Ruey-Shiuan, Bernard Testa, Nabil El Tayar, and Pierre-Alain Carrupt. "Structure–lipophilicity relationships of zwitterionic amino acids." J. Chem. Soc., Perkin Trans. 2, no. 11 (1991): 1797–802. http://dx.doi.org/10.1039/p29910001797.

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Wang, P., M. Reed, Y. Wang, et al. "p53 domains: structure, oligomerization, and transformation." Molecular and Cellular Biology 14, no. 8 (1994): 5182–91. http://dx.doi.org/10.1128/mcb.14.8.5182.

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Wild-type p53 forms tetramers and multiples of tetramers. Friedman et al. (P. N. Friedman, X. B. Chen, J. Bargonetti, and C. Prives, Proc. Natl. Acad. Sci. USA 90:3319-3323, 1993) have reported that human p53 behaves as a larger molecule during gel filtration than it does during sucrose gradient sedimentation. These differences argue that wild-type p53 has a nonglobular shape. To identify structural and oligomerization domains in p53, we have investigated the physical properties of purified segments of p53. The central, specific DNA-binding domain within murine amino acids 80 to 320 and human

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Wang, P., M. Reed, Y. Wang, et al. "p53 domains: structure, oligomerization, and transformation." Molecular and Cellular Biology 14, no. 8 (1994): 5182–91. http://dx.doi.org/10.1128/mcb.14.8.5182-5191.1994.

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Wild-type p53 forms tetramers and multiples of tetramers. Friedman et al. (P. N. Friedman, X. B. Chen, J. Bargonetti, and C. Prives, Proc. Natl. Acad. Sci. USA 90:3319-3323, 1993) have reported that human p53 behaves as a larger molecule during gel filtration than it does during sucrose gradient sedimentation. These differences argue that wild-type p53 has a nonglobular shape. To identify structural and oligomerization domains in p53, we have investigated the physical properties of purified segments of p53. The central, specific DNA-binding domain within murine amino acids 80 to 320 and human

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Heinicke, Joachim, Joanna Lach, Kaleswara R. Basvani, Normen Peulecke, Peter G. Jones та Martin Köckerling. "α-Phosphino Amino Acids: Synthesis, Structure, and Reactivity". Phosphorus, Sulfur, and Silicon and the Related Elements 186, № 4 (2011): 666–77. http://dx.doi.org/10.1080/10426507.2010.514485.

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Smith, Martin D., Timothy D. W. Claridge, George W. J. Fleet, George E. Tranter, and Mark S. P. Sansom. "Secondary structure in oligomers of carbohydrate amino acids." Chemical Communications, no. 18 (1998): 2041–42. http://dx.doi.org/10.1039/a805401k.

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CHEON, MOOKYUNG, MUYOUNG HEO, IKSOO CHANG, and CHOONGRAK KIM. "CLASSIFICATIONS OF AMINO ACIDS IN PROTEINS BY THE SELF-ORGANIZING MAP." International Journal of Modern Physics C 16, no. 10 (2005): 1609–16. http://dx.doi.org/10.1142/s0129183105008175.

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We present the clustering properties of amino acids, which are building blocks of proteins, according to their physico-chemical characters. To classify the 20 kinds of amino acids, we employ a Self-Organizing Map (SOM) analysis for the Miyazawa-Jernigan (MJ) pairwise-contact matrix, the Environment-dependent One-body energy Parameters (EOP) and the one-body energy parameters incorporating the Ramachandran angle information (EOPR) over the EOP in proteins. We provide the new result of the SOM clustering for amino acids based on the EOPR and compare that with those from the MJ and the EOP matrix

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Dissertations / Theses on the topic "Amino acids - Structure"

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Malešević, Miroslav. "[Beta]-amino [Beta-amino] acids as secondary structure inducers in peptides." [S.l. : s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=966017811.

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Lin, Guoliang. "NOVEL METHANOPYRROLIDINE β– AMINO ACIDS". Diss., Temple University Libraries, 2010. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/92631.

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Chemistry<br>Ph.D.<br>Methanopyrrolidine-5-carboxylic acids (MetPyr-5-acids), or 5-syn-carboxy-2- azabicyclo[2.1.1]hexanes are building blocks for β-peptides that cannot form backbone hydrogen bonds. To introduce functionality to this ring system, 6-syn-benzyloxymethyl and 6-syn-phenyl substituted derivatives have been prepared by an efficient synthetic procedure. Addition of appropriately substituted allyl amines to 3-butynone, amide protection, and irradiation afford mainly 5-acetyl-2-azabicyclo[2.1.1]hexanes. Haloform oxidation leads to the desired 6-substituted MetPyr-5-acids. A 1-ethoxyca

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Li, Bing, and 李兵. "Aminoxy acids as building blocks for turns and helices." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2000. http://hub.hku.hk/bib/B31240549.

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Sweet, Miles J. "Applications of ÃŸ-amino acids in synthesis and structure." Thesis, University of Oxford, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.418131.

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吳飛虎 and Fei-fu Ng. "An unusual turn structure in peptides containing alpha-aminoxyacids." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1998. http://hub.hku.hk/bib/B31219731.

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Ng, Fei-fu. "An unusual turn structure in peptides containing alpha-aminoxyacids /." Hong Kong : University of Hong Kong, 1998. http://sunzi.lib.hku.hk/hkuto/record.jsp?B19945747.

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Eastwood, Amy Lynn Gray Harry B. Dougherty Dennis A. "Investigating structure-function relationships in ion channels using unatural amino acids /." Diss., Pasadena, Calif. : California Institute of Technology, 2009. http://resolver.caltech.edu/CaltechETD:etd-01062009-133603.

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Halonski, John. "Utilization of Unnatural Amino Acids to Modulate Protein Structure and Function." W&M ScholarWorks, 2018. https://scholarworks.wm.edu/etd/1530192786.

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Proteins are capable of an astounding array of functions using only the 20 canonical amino acids; however, the ability to add new functional groups to the genetic code through the utilization of unnatural amino acids (UAAs) has greatly expanded our ability to study and manipulate proteins. By expanding the diversity of functional groups within proteins, a wide variety of applications in industry as well as in fields such as diagnostics, biochemistry, and materials science are now possible. These applications have further been expanded through the development and optimization of bioorthogonal r

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Baktula, Avinash M. "A Method Based on Conserved Multiple Amino Acid Properties to Predict Amino Acid Substitutions Which Maintain the Protein Structure." TopSCHOLAR®, 2004. http://digitalcommons.wku.edu/theses/1107.

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A METHOD BASED ON CONSERVED MULTIPLE AMINO ACID PROPERTIES TO PREDICT AMINO ACID SUBSTITUTIONS WHICH MAINTAIN THE PROTEIN STRUCTURE Avinash M. Baktula September 16, 2004 1-117 Directed by: Claire A. Rinehart, Doug McElroy and Sigrid Jacobshagen Department of Biology Western Kentucky University Proteins often contain several domains, each with a distinct structure. Such domains have evolved as units that, when combined in various arrangements, produce proteins of unique structure. This study was conducted to identify amino acid substitutions that don’t change structure. Amino acid properties wh

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Sutherland, Andrew. "The enantioselective synthesis of amino acids for the investigation of protein structure." Thesis, University of Bristol, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388029.

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Books on the topic "Amino acids - Structure"

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Gurskaya, Galina V. The Molecular Structure of Amino Acids. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4684-1566-7.

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Sillince, John A. A. Molecular Databases for Protein Sequences and Structure Studies: An Introduction. Springer Berlin Heidelberg, 1991.

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Taylor, William R. Patterns in Protein Sequence and Structure. Springer Berlin Heidelberg, 1992.

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John, Tooze, ed. Introduction to protein structure. Garland Pub., 1991.

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John, Tooze, ed. Introduction to protein structure. 2nd ed. Garland Pub., 1999.

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Brändén, Carl-Ivar. Introduction to protein structure. 2nd ed. Garland Pub., 2009.

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7

Ellson, D. A. Electronic structure calculations of amino acid radicals. UMIST, 1997.

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Nordlund, Pär. Structural studies on the free radical protein of ribonucleotide reductase. Dept. of Molecular Biology, Swedish University of Agricultural Sciences, 1990.

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Lorne Conference on Protein Structure & Function (28th 2003). 28th Annual Lorne Conference on Protein Structure & Function: Sun. 9 - Thurs. 13 February 2003. s.n., 2003.

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International Symposium on Protein Structure-Function Relationship (1988 Karachi, Pakistan). Protein structure-function relationship: Proceedings of the International Symposium on Protein Structure-Function Relationship, held in Karachi, Pakistan, 18-20 January 1988, and of the Protein Sequencing Workshop, held subsequently in Karachi, Pakistan, 21-30 January 1988. Edited by Zaidi Zafar H and Protein Sequencing Workshop (1988 : Karachi, Pakistan). Elsevier Science Publishers, 1988.

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Book chapters on the topic "Amino acids - Structure"

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Buxbaum, Engelbert. "Amino Acids." In Fundamentals of Protein Structure and Function. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-19920-7_1.

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Yohda, Masafumi. "Aspartate Racemase: Function, Structure, and Reaction Mechanism." In D-Amino Acids. Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-56077-7_21.

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Waldron, Karen C., Michael Carpenter, Ian Ireland, Darren Lewis, Xing Fang Li, and Norman J. Dovichi. "High Sensitivity Analysis of PTH Amino Acids." In Methods in Protein Structure Analysis. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1031-8_5.

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Pisano, Anthony, Nicolle H. Packer, John W. Redmond, Keith L. Williams, and Andrew A. Gooley. "Identification and Characterization of Glycosylated Phenylthiohydantoin Amino Acids." In Methods in Protein Structure Analysis. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1031-8_7.

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Zhao, Yu-Fen, and Pei-sheng Cao. "Phosphoryl amino acids: Common origin for nucleic acids and protein." In Chemical Evolution: Structure and Model of the First Cell. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0105-9_31.

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Vollenbroich, D., and K. Krause. "Quantitative Analysis of D- and L-Amino Acids by HPLC." In Protein Structure Analysis. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59219-5_16.

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Page, Michael I. "Structure and Reactivity of β-Lactams." In Amino Acids, Peptides and Proteins in Organic Chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527631803.ch5.

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Campo, Marino A., Jaime Escalante та Radovan Šebesta. "β2-Amino Acids with Proteinogenic Side Chains and Corresponding Peptides: Synthesis, Secondary Structure, and Biological Activity". У Enantioselective Synthesis of β-Amino Acids. John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471698482.ch23.

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Norton, Raymond S. "Structure and Activity of N-Methylated Peptides." In Amino Acids, Peptides and Proteins in Organic Chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527631841.ch4.

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Fisher, Andrew J. "X-Ray Structure Determination of Proteins and Peptides." In Amino Acids, Peptides and Proteins in Organic Chemistry. Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527631841.ch2.

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Conference papers on the topic "Amino acids - Structure"

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Joshi, S. K., V. K. Hinge, and B. D. Shrivastava. "EXAFS Studies of Cobalt(II) Complexes with Amino Acids." In X-RAY ABSORPTION FINE STRUCTURE - XAFS13: 13th International Conference. AIP, 2007. http://dx.doi.org/10.1063/1.2644518.

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Sumi, Y., Y. Nakamura, M. Sakai, M. Muramatsu та N. Aoki. "STRUCTURE OF HUMAN α2-PLASMIN INHIBITOR DEDUCED FROM THAT OF cDNA". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644371.

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The complete amino acid sequence of α2-plasmin inhibitor (α2PI) was determined by cDNA cloning. A Agt 10 cDNA library was prepared from poly(A)+mRNA isolated from cultured human liver cells. The labeled oligonucleotides, corresponding to the reported partial amino acid sequences of α2PI, were used as probes to screen the library. One of the positive clones was subcloned into plasmid pUC8. A 2.2 kilobase cDNA clone thus isolated contains a region coding for a portion of a leader sequence, the mature protein, a stop codon (TGA), a 3' noncoding region (733 nucleotides), and a poly(A)tail (37 nucl

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Katti, Kalpana S., Dinesh R. Katti, and Avinash H. Ambre. "Unnatural Amino Acids Modified Clays for Design of Scaffolds for Bone Tissue Engineering." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13242.

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Here, we incorporate the results of our new “altered phase theory” (Sikdar et al. 2008a) into design of new polymer clay nanocomposites (PCNs) for bone biomaterials applications. Montmorillonite (MMT) clay was modified using unnatural amino acids as potentially new biocompatible modifiers. The longer carbon chain structures of the unnatural amino acids are expected to enhance non bonded interactions with clay as well as maintaining the usefulness of functional groups of natural amino acids. The specific choice of amino acids is based on both the antibacterial activity reported in literature an

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Heckel, A., and K. M. Hasselbach. "PREDICTION OF THE THREE-DIMENSIONAL STRUCTURE OF THE ENZYMATIC PART OF T-PA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644407.

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Up to now the three-dimensional structure of t-PA or parts of this enzyme is unknown. Using computer graphical methods the spatial structure of the enzymatic part of t-PA is predicted on the hypothesis, the three-dimensional backbone structure of t-PA being similar to that of other serine proteases. The t-PA model was built up in three steps:1) Alignment of the t-PA sequence with other serine proteases. Comparison of enzyme structures available from Brookhaven Protein Data Bank proved elastase as a basis for modeling.2) Exchange of amino acids of elastase differing from the t-PA sequence. The

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Jenny, Richard J., Debra D. Pittman, John J. Toole, Ronald W. Kriz, Randal J. Kaufman, and Kenneth G. Mann. "THE COMPLETE AMINO ACID SEQUENCE OF HUMAN FACTOR V." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643887.

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cDNA clones encoding human factor V have been isolated and sequenced. The cDNA sequence of factor V obtained from overlapping clones includes a 6672 bp coding region, a 90 bp 5'-untranslated region and a 163 bp 3’-untranslated region including a poly-A tail. The deduced amino acid sequence consists of 2224 amino acids including a 28 amino acid leader peptide. A direct comparison to human factor VIII reveals considerable homology between both proteins with respect to amino acid sequence and domain structure. A triplicated "A" domain and duplicated "C" domain show an approximate 40% identity to

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Chatterjee, Piyali, Subhadip Basu, and Mita Nasipuri. "Improving prediction of protein secondary structure using physicochemical properties of amino acids." In the International Symposium. ACM Press, 2010. http://dx.doi.org/10.1145/1722024.1722036.

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ISMAILOV, Ismail Sagidovich, Nina Vladimirovna TREGUBOVA, Rashid Hasanbievich KOCHKAROV, Anna Victorovna MORGUNOVA, and Natalija Alecseevna DRIZHD. "THE RELATIONSHEEP OF AMINO ACID METABOLISM WITH PRODUCTIVITY OF GROWING YOUNG SHEEP." In RURAL DEVELOPMENT. Aleksandras Stulginskis University, 2018. http://dx.doi.org/10.15544/rd.2017.125.

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A number of studies on digestion of the ruminants have shown the process of synthesis of all the essential amino acids in the rumen (Abu Fadel, 2004; Trukhachev, V., Zlidnev, N. 2008). However, according to some researches, microbial protein is deficient in methionine and lysine. This assumption also proves the need for further study of the influence of balanced amino acids to these diets on the growth, development and productive performance of the ruminants. Scientific approbation of the issues related to establishing the requirements of young sheep in lysine and methionine with cystine and d

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Butler-Zimrin, A. E., J. S. Bennett, M. Poncz, et al. "ISOLATION AND CHARACTERIZATION OF cDNA CLONES FOR THE PLATELET MEMBRANE GLYCOPROTEINS IIb and IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643961.

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The platelet membrane GPIIb/GPIIIa complex on activated platelets contains receptors for fibrinogen, von Willebrand factor, and fibronectin. GPIIb and GPIlia also appear to be members of a family of membrane receptors involved in cell-cell and cell-matrix interactions. To study the structure of GPIIb and GPIIIa, we have constructed an expression library in the vector lambda gtll using mRNA from the HEL cell line and screened it with polyclonal antibody against each platelet protein. HEL cells constitutively express proteins similar to platelet GPIIb and GPIIIa. A 3.2kb GPIIb cDNA clone was ide

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Liu, Danyi, and Edwin van der Heide. "Interactive Auditory Navigation in the Molecular Structures of Amino Acids: A Case Study Using Multiple Concurrent Sound Sources Representing Nearby Atoms." In ICAD 2019: The 25th International Conference on Auditory Display. Department of Computer and Information Sciences, Northumbria University, 2019. http://dx.doi.org/10.21785/icad2019.049.

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We are interested in sonifying the molecular structures of amino acids. This paper describes the context and the ﬁrst design choices for our approach. So far, we believe an amino acid molecule is too complex to be perceived at once. Therefore, we have designed an interactive form of soniﬁcation in which the listener navigates through the molecule over the network of carbon atoms. We describe our different approaches and discuss the topic of immediacy: the time it takes to recognize the structure surrounding the listener’s position while navigating. Furthermore, we touch upon the question how m

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Nottingham, Elizabeth M., Michelle G. Zeles-Hahn, and Corinne S. Lengsfeld. "Understanding EHDA and Protein Stability." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176708.

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Therapeutic proteins can be difficult to work with due to the fact that each protein has properties and functions that are unique. These exclusive properties are in part due to the proteins three-dimensional shape (secondary and tertiary structure). This shape is determined by bends in the amino acid sequence generated by electrostatic interactions, hydrogen bonds, and hydrophobic-hydrophilic interactions between neighboring amino acids. These bonding interactions are weak and can be severed by chemical or physical forces. Thus, therapeutic proteins can be denatured during manufacture and by m

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