Propensities of Aromatic Amino Acids versus Leucine and Proline to Induce Residual Structure in the Denatured-State Ensemble of Iso-1-cytochrome c

Journal of Molecular Biology

Volumn 403, Issue 4, 2010, Pages 495-504

  Finnegan, Michaela L ^a   Bowler, Bruce E ^a  

^a UNIVERSITY OF MONTANA   (United States)

Author keywords

Chain stiffness; Denatured states; Loop formation; Protein folding; Residual structure

Indexed keywords

ALANINE; AROMATIC AMINO ACID; CYTOCHROME C; GUANIDINE; HISTIDINE; ISOCYTOCHROME C1; LEUCINE; LYSINE; PHENYLALANINE; PROLINE; TRYPTOPHAN; UNCLASSIFIED DRUG; CYC1 PROTEIN, S CEREVISIAE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; KINETICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; YEAST; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN ENGINEERING; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY;

AMINO ACID SUBSTITUTION; AMINO ACIDS, AROMATIC; CYTOCHROMES C; KINETICS; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROLINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STABILITY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 77957918625     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.09.004     Document Type: Article

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