Long-range intra-protein communication can be transmitted by correlated side-chain fluctuations alone

PLoS Computational Biology

Volumn 7, Issue 9, 2011, Pages

  DuBay, Kateri H ^a,b,c   Bothma, Jacques P ^a   Geissler, Phillip L ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^c Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAINS; HYDROGEN BONDS; MONTE CARLO METHODS;

ALLOSTERIC REGULATION; CHAIN MOTIONS; FOLDED PROTEINS; INFORMATION CONVEYANCE; LONG RANGE CORRELATIONS; MONTE CARLO SAMPLING; POTENTIAL UTILITY; RANGE INFORMATION; SIDE-CHAINS; TORSIONAL ANGLE;

CALMODULIN;

CALMODULIN; BACTERIAL PROTEIN; BARSTAR PROTEIN, BACILLUS AMYLOLIQUEFACIENS; PROTEIN; SOLVENT;

ARTICLE; CELL COMMUNICATION; CONTROLLED STUDY; ENTROPY; HYDROGEN BOND; MATHEMATICAL MODEL; MOLECULAR INTERACTION; MONTE CARLO METHOD; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; STEREOSPECIFICITY; ALLOSTERISM; BINDING SITE; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN DOMAIN; PROTEIN FOLDING;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BINDING SITES; CALMODULIN; COMPUTATIONAL BIOLOGY; COMPUTER SIMULATION; HYDROGEN BONDING; MODELS, MOLECULAR; MONTE CARLO METHOD; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEINS; SOLVENTS;

EID: 80053443092     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002168     Document Type: Article

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