Probing the Flexibility of Large Conformational Changes in Protein Structures through Local Perturbations

PLoS Computational Biology

Volumn 5, Issue 4, 2009, Pages

  Ho, Bosco K ^a   Agard, David A ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL EFFICIENCY; LIGANDS; MOLECULAR DYNAMICS; PERTURBATION TECHNIQUES; PROTEINS;

CONFORMATIONAL CHANGE; CONFORMATIONAL DYNAMICS; DEFORMATION MAP; DYNAMIC BEHAVIORS; GLOBAL MAP; LIGAND BINDING; LOCAL PERTURBATION; PROTEIN CONFORMATIONAL CHANGES; PROTEINS STRUCTURES; STRUCTURAL ELEMENTS;

DEFORMATION;

DIHYDROFOLATE REDUCTASE; ESTROGEN RECEPTOR; PROTEINASE; TRIOSEPHOSPHATE ISOMERASE;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; LIGAND BINDING; MODULATION; MOLECULAR DYNAMICS; MOTION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SURFACE PROPERTY; AMINO ACID SEQUENCE; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; METHODOLOGY; MOLECULAR GENETICS; SEQUENCE ANALYSIS; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ANALYSIS, PROTEIN; TRIOSE-PHOSPHATE ISOMERASE;

EID: 65349192770     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000343     Document Type: Article

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