Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?

The prevailing current view of protein folding is the thermodynamic hypothesis, under which the native folded conformation of a protein corresponds to the global minimum of Gibbs free energy G. We question this concept and show that the empirical evidence behind the thermodynamic hypothesis of foldi...

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Bibliographic Details
Published in:	International journal of molecular sciences Vol. 23; no. 1; p. 521
Main Authors:	Sorokina, Irina, Mushegian, Arcady R., Koonin, Eugene V.
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 04.01.2022 MDPI
Subjects:	Algorithms Enzymes Experiments Hypotheses Kinetics Models, Molecular Models, Theoretical Protein Conformation Protein Folding Protein Refolding Protein Stability Proteins - chemical synthesis Proteins - chemistry Proteome Proteomics - methods Recombinant Proteins - chemistry Review Solubility Species Specificity Thermodynamics energy-dependent protein folding entropy co-translational protein folding free energy physical model of protein folding protein folding molecular chaperones free energy landscape
ISSN:	1422-0067, 1661-6596, 1422-0067
Online Access:	Get full text
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