Abstract
We introduce a simple theoretical approach for an equilibrium study of proteins with known native-state structures. We test our approach with results on well-studied globular proteins, chymotrypsin inhibitor (2ci2), barnase, and the alpha spectrin SH3 domain, and present evidence for a hierarchical onset of order on lowering the temperature with significant organization at the local level even at high temperatures. A further application to the folding process of HIV-1 protease shows that the model can be reliably used to identify key folding sites that are responsible for the development of drug resistance.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Bacterial Proteins
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Biophysical Phenomena
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Biophysics
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Chemical Phenomena
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Chemistry, Physical
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HIV Protease / chemistry
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Humans
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In Vitro Techniques
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Models, Chemical
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Peptides
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Plant Proteins / chemistry
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Protein Conformation*
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Protein Folding
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Protein Structure, Tertiary
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Proteins / chemistry*
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Ribonucleases / chemistry
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Spectrin / chemistry
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Thermodynamics
Substances
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Bacterial Proteins
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Peptides
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Plant Proteins
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Proteins
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chymotrypsin inhibitor 2
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Spectrin
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Ribonucleases
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Bacillus amyloliquefaciens ribonuclease
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HIV Protease