Shortening a loop can increase protein native state entropy

Proteins: Structure, Function and Bioinformatics

Volumn 83, Issue 12, 2015, Pages 2137-2146

  Gavrilov, Yulian ^a   Dagan, Shlomi ^a   Levy, Yaakov ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Coarse grained model; Conformational entropy; Molecular dynamics; Native state dynamics; Protein folding

Indexed keywords

ACYLPHOSPHATASE; MUTANT PROTEIN; PROTEIN; PROTEIN UBC7; SOLVENT; UNCLASSIFIED DRUG; ACID ANHYDRIDE HYDROLASE; SACCHAROMYCES CEREVISIAE PROTEIN; SPECTRIN; UBC7 PROTEIN, S CEREVISIAE; UBIQUITIN CONJUGATING ENZYME;

ARTICLE; CONTROLLED STUDY; ENTROPY; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN UNFOLDING; SOLVENT EFFECT; THERMODYNAMICS; THERMOSTABILITY; CHEMISTRY; METABOLISM; PROTEIN CONFORMATION; SRC HOMOLOGY DOMAIN;

ACID ANHYDRIDE HYDROLASES; ENTROPY; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTRIN; SRC HOMOLOGY DOMAINS; UBIQUITIN-CONJUGATING ENZYMES;

EID: 84954383307     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24926     Document Type: Article

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