Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: Contribution of His41 to the pH-dependent stability of the N-terminal subdomain

Journal of Molecular Biology

Volumn 355, Issue 5, 2006, Pages 1078-1094

  Grey, Michael J ^a   Tang, Yuefeng ^b   Alexov, Emil ^c   McKnight, C James ^d   Raleigh, Daniel P ^b   Palmer III, Arthur G ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b STONY BROOK UNIVERSITY   (United States)

^c CLEMSON UNIVERSITY   (United States)

^d BOSTON UNIVERSITY   (United States)

Author keywords

Chemical exchange; pH dependent stability; Protein folding; Relaxation dispersion; Villin headpiece domain

Indexed keywords

HISTIDINE; IMIDAZOLE; VILLIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; ENERGY; MOLECULAR INTERACTION; NITROGEN NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SOLVATION; STRUCTURE ANALYSIS;

EID: 29444454319     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.11.001     Document Type: Article

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