Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 43, 2014, Pages 15396-15401

  Baxa, Michael C ^a,b   Haddadian, Esmael J ^a   Jumper, John M ^c   Freed, Karl F ^a,c   Sosnick, Tobin R ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

^c UNIVERSITY OF CHICAGO   (United States)

Author keywords

Helix propensity; Molecular dynamics; NMR order parameters; Sheet propensity denatured state

Indexed keywords

AMIDE; CARBONYL DERIVATIVE; UBIQUITIN; AMINO ACID;

ARTICLE; CHEMICAL BOND; ENTROPY; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; THERMODYNAMICS; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACIDS; ENTROPY; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; UBIQUITIN;

EID: 84908288276     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1407768111     Document Type: Article

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