Positive and negative design in stability and thermal adaptation of natural proteins

10.1371/journal.pcbi.0030052

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Bibliographic Details
Main Authors:	Berezovsky I.N., Zeldovich K.B., Shakhnovich E.I.
Other Authors:	BIOLOGICAL SCIENCES
Format:	Article
Published:	2019
Subjects:	proteome archaeal protein amino acid composition amino acid sequence article environmental factor hydrophobicity molecular model mutation protein analysis protein conformation protein folding protein interaction protein stability protein structure temperature dependence chemical model chemical phenomena chemical structure chemistry computer simulation drug stability methodology molecular genetics protein denaturation sequence alignment sequence analysis structure activity relation temperature ultrastructure Amino Acid Sequence Archaeal Proteins Computer Simulation Drug Stability Hydrophobic and Hydrophilic Interactions Models, Chemical Models, Molecular Molecular Sequence Data Protein Denaturation Protein Folding Sequence Alignment Sequence Analysis, Protein Structure-Activity Relationship Temperature
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/161869
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1618692024-04-03T10:11:57Z Positive and negative design in stability and thermal adaptation of natural proteins Berezovsky I.N. Zeldovich K.B. Shakhnovich E.I. BIOLOGICAL SCIENCES proteome archaeal protein amino acid composition amino acid sequence article environmental factor hydrophobicity molecular model mutation protein analysis protein conformation protein folding protein interaction protein stability protein structure temperature dependence chemical model chemical phenomena chemical structure chemistry computer simulation drug stability methodology molecular genetics protein denaturation sequence alignment sequence analysis structure activity relation temperature ultrastructure Amino Acid Sequence Archaeal Proteins Computer Simulation Drug Stability Hydrophobic and Hydrophilic Interactions Models, Chemical Models, Molecular Molecular Sequence Data Protein Denaturation Protein Folding Sequence Alignment Sequence Analysis, Protein Structure-Activity Relationship Temperature 10.1371/journal.pcbi.0030052 PLoS Computational Biology 3 3 498-507 2019-11-08T00:59:39Z 2019-11-08T00:59:39Z 2007 Article Berezovsky I.N., Zeldovich K.B., Shakhnovich E.I. (2007). Positive and negative design in stability and thermal adaptation of natural proteins. PLoS Computational Biology 3 (3) : 498-507. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pcbi.0030052 1553734X https://scholarbank.nus.edu.sg/handle/10635/161869 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20191101
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	proteome archaeal protein amino acid composition amino acid sequence article environmental factor hydrophobicity molecular model mutation protein analysis protein conformation protein folding protein interaction protein stability protein structure temperature dependence chemical model chemical phenomena chemical structure chemistry computer simulation drug stability methodology molecular genetics protein denaturation sequence alignment sequence analysis structure activity relation temperature ultrastructure Amino Acid Sequence Archaeal Proteins Computer Simulation Drug Stability Hydrophobic and Hydrophilic Interactions Models, Chemical Models, Molecular Molecular Sequence Data Protein Denaturation Protein Folding Sequence Alignment Sequence Analysis, Protein Structure-Activity Relationship Temperature
spellingShingle	proteome archaeal protein amino acid composition amino acid sequence article environmental factor hydrophobicity molecular model mutation protein analysis protein conformation protein folding protein interaction protein stability protein structure temperature dependence chemical model chemical phenomena chemical structure chemistry computer simulation drug stability methodology molecular genetics protein denaturation sequence alignment sequence analysis structure activity relation temperature ultrastructure Amino Acid Sequence Archaeal Proteins Computer Simulation Drug Stability Hydrophobic and Hydrophilic Interactions Models, Chemical Models, Molecular Molecular Sequence Data Protein Denaturation Protein Folding Sequence Alignment Sequence Analysis, Protein Structure-Activity Relationship Temperature Berezovsky I.N. Zeldovich K.B. Shakhnovich E.I. Positive and negative design in stability and thermal adaptation of natural proteins
description	10.1371/journal.pcbi.0030052
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Berezovsky I.N. Zeldovich K.B. Shakhnovich E.I.
format	Article
author	Berezovsky I.N. Zeldovich K.B. Shakhnovich E.I.
author_sort	Berezovsky I.N.
title	Positive and negative design in stability and thermal adaptation of natural proteins
title_short	Positive and negative design in stability and thermal adaptation of natural proteins
title_full	Positive and negative design in stability and thermal adaptation of natural proteins
title_fullStr	Positive and negative design in stability and thermal adaptation of natural proteins
title_full_unstemmed	Positive and negative design in stability and thermal adaptation of natural proteins
title_sort	positive and negative design in stability and thermal adaptation of natural proteins
publishDate	2019
url	https://scholarbank.nus.edu.sg/handle/10635/161869
_version_	1795374118845022208

Positive and negative design in stability and thermal adaptation of natural proteins

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