Thermodynamics and kinetics of non-native interactions in protein folding: A single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state

Journal of Molecular Biology

Volumn 338, Issue 4, 2004, Pages 827-837

  Cho, Jae Hyun ^a   Sato, Satoshi ^a,b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b MRC CENTRE FOR PROTEIN ENGINEERING   (United Kingdom)

Author keywords

Denatured state; K12M, NTL9, the K12M mutant of NTL9; kch, the intrinsic rate of amide proton exchange; Non native interactions; NTL9, the first 56 residues of the ribosomal protein L9; pH dependent folding; Protein folding; Protein stability

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL REACTION KINETICS; DENATURATION; MUTATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 1942521649     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.073     Document Type: Article

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