Thermal Stabilization of Dihydrofolate Reductase Using Monte Carlo Unfolding Simulations and Its Functional Consequences

PLoS Computational Biology

Volumn 11, Issue 4, 2015, Pages

  Tian, Jian ^a,b   Woodard, Jaie C ^c   Whitney, Anna ^a   Shakhnovich, Eugene I ^a  

^a HARVARD UNIVERSITY   (United States)

^b INSTITUTE OF PLANT PROTECTION   (China)

^c HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; ENZYME ACTIVITY; ESCHERICHIA COLI; MONTE CARLO METHODS; MUTAGENESIS; STABILITY;

ACTIVE SITE; BIOTECHNOLOGICAL APPLICATIONS; DENATURATION TEMPERATURES; DIHYDROFOLATE REDUCTASE; NON EQUILIBRIUM; PROTEIN STABILITY; SCIENTIFIC APPLICATIONS; THEORETICAL APPROACH; THERMAL STABILIZATION; UNFOLDINGS;

MELTING POINT;

DIHYDROFOLATE REDUCTASE;

ARTICLE; CATALYSIS; CONCEPTUAL FRAMEWORK; CONTROLLED STUDY; ENTROPY; ESCHERICHIA COLI; GENE MUTATION; MELTING POINT; MEMBRANE STABILIZATION; MONTE CARLO METHOD; MUTAGENESIS; NONHUMAN; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN UNFOLDING; SIMULATION; TEMPERATURE; THERMOSTABILITY; CHEMICAL MODEL; CHEMISTRY; COMPUTER SIMULATION; ENZYME STABILITY; GENETICS; MOLECULAR MODEL; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS; STATISTICAL MODEL; STRUCTURE ACTIVITY RELATION; TRANSITION TEMPERATURE; ULTRASTRUCTURE;

COMPUTER SIMULATION; ENZYME STABILITY; MODELS, CHEMICAL; MODELS, MOLECULAR; MODELS, STATISTICAL; MONTE CARLO METHOD; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; TETRAHYDROFOLATE DEHYDROGENASE; TRANSITION TEMPERATURE;

EID: 84929497890     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1004207     Document Type: Article

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