Mutational studies of protein stability and folding of the hyperstable MYL Arc repressor variant

Biophysical Chemistry

Volumn 101-102, Issue , 2002, Pages 35-42

  Srivastava, Alok K ^a   Sauer, Robert T ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Arc MYL variant; Buried salt bridge; Context dependence; Fast folding mutants; Transition state

Indexed keywords

PROTEIN; PROTEIN ARC MYL; UNCLASSIFIED DRUG; NUCLEAR PROTEIN; PHAGE REPRESSOR PROTEINS; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TUMOR PROTEIN; TUMOR SUPPRESSOR PROTEIN; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; HYDROPHOBICITY; KINETICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; PROTEIN CONFORMATION;

KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NEOPLASM PROTEINS; NUCLEAR PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; REPRESSOR PROTEINS; TRANSCRIPTION FACTORS; TUMOR SUPPRESSOR PROTEINS; VIRAL PROTEINS;

EID: 0037059034     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00180-1     Document Type: Article

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