Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding

Journal of Molecular Biology

Volumn 345, Issue 1, 2005, Pages 163-173

  Horng, Jia Cherng ^a   Cho, Jae Hyun ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

linkage relationship; protein folding; protein stability; ribosomal protein L9; values

Indexed keywords

HISTIDINE; RIBOSOME PROTEIN; RIBOSOME PROTEIN L9; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CALCULATION; CARBOXY TERMINAL SEQUENCE; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTON TRANSPORT; THERMODYNAMICS;

EID: 9644303208     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.023     Document Type: Article

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