Are Current Atomistic Force Fields Accurate Enough to Study Proteins in Crowded Environments?

PLoS Computational Biology

Volumn 10, Issue 5, 2014, Pages

  Petrov, Drazen ^a   Zagrovic, Bojan ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; IONIC STRENGTH; MOLECULAR DYNAMICS; MOLECULAR PHYSICS; POTENTIAL ENERGY; STABILITY;

'CURRENT; ATOMISTICS; CELLULARS; DYNAMICS SIMULATION; FORCEFIELDS; PROTEIN BEHAVIOR; PROTEIN CONCENTRATIONS; THERMODYNAMICS AND KINETICS; VILLIN HEADPIECE; WILD TYPES;

PROTEINS;

PROTEIN DERIVATIVE; SOLVENT; VILLIN; WATER; ACTIN BINDING PROTEIN;

ACCURACY; ARTICLE; CONTROLLED STUDY; FORCE; HYDROPHOBICITY; IONIC STRENGTH; MOLECULAR DYNAMICS; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEFECT; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; PROTEIN UNFOLDING; SIMULATION; STATIC ELECTRICITY; WATER PROTEIN INTERACTION; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; MECHANICAL STRESS; PROTEIN CONFORMATION; PROTEIN FOLDING; ULTRASTRUCTURE;

MICROFILAMENT PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; STRESS, MECHANICAL;

EID: 84901675920     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003638     Document Type: Article

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