The fast-folding HP35 double mutant has a substantially reduced primary folding free energy barrier

Journal of Chemical Physics

Volumn 129, Issue 15, 2008, Pages

  Lei, Hongxing ^a,b   Deng, Xiaojian ^b   Wang, Zhixiang ^b,c   Duan, Yong ^b  

^a Chinese Academy of Sciences and China National Center for Bioinformation   (China)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DYNAMICS; ENERGY BARRIERS; FREE ENERGY; MELTING POINT; MOLECULAR DYNAMICS; QUANTUM CHEMISTRY;

AB INITIO; CONSISTENT; DENATURED STATES; DOUBLE MUTANTS; DOWNHILL FOLDING; ELECTROSTATIC INTERACTIONS; FOLDED CONFORMATIONS; FOLDED STATES; FOLDING MECHANISMS; FOLDING PROCESSES; FOLDING TIMES; FOLDING TRANSITIONS; FORCE FIELDS; INTERMEDIATE STATES; MELTING TEMPERATURES; MUTATIONAL EFFECTS; NATIVE STATES; REPLICA EXCHANGE MOLECULAR DYNAMICS; ROOT MEAN SQUARED; SECONDARY STRUCTURES; SOLVATION MODELS; SUBDOMAIN; TRANSITION BARRIERS; TRANSITION STATE ENSEMBLES; TRANSITION STATES; VILLIN HEADPIECES; WILD TYPES;

PROTEIN FOLDING;

ACTIN BINDING PROTEIN; MUTANT PROTEIN; PEPTIDE FRAGMENT; VILLIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; QUANTUM THEORY; TEMPERATURE; THERMODYNAMICS; TIME;

KINETICS; MICROFILAMENT PROTEINS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; QUANTUM THEORY; TEMPERATURE; THERMODYNAMICS; TIME FACTORS;

EID: 54849428346     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.2995987     Document Type: Article

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