Microsecond simulations of the folding/ unfolding thermodynamics of the Trp-cage miniprotein

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 8, 2010, Pages 1889-1899

  Day, Ryan ^a   Paschek, Dietmar ^a   Garcia, Angel E ^a  

^a Research Rensselaer Polytechnic Institute   (United States)

Author keywords

Cold denaturation; Folding; Force field; Molecular simulations; Pressure denaturation

Indexed keywords

GLOBULAR PROTEIN; TRP CAGE MINIPROTEIN; UNCLASSIFIED DRUG;

ARTICLE; DENATURATION; ENERGY TRANSFER; ENTHALPY; ENTROPY; FORCE; HEAT; HIGH TEMPERATURE; HYDROGEN BOND; LOW TEMPERATURE; MOLECULAR DYNAMICS; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FOLDING; TEMPERATURE DEPENDENCE; THERMODYNAMICS; TRANSITION TEMPERATURE;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS; TIME FACTORS;

EID: 77953508894     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22702     Document Type: Article

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