The Folding Energy Landscape of the Dimerization Domain of Escherichia coli Trp Repressor: A Joint Experimental and Theoretical Investigation

Journal of Molecular Biology

Volumn 363, Issue 1, 2006, Pages 262-278

  Simler, B Robert ^a   Levy, Yaakov ^b   Onuchic, José N ^b   Matthews, C Robert ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

G model; hydrogen exchange; mass spectrometry; protein folding; segment swapping

Indexed keywords

DIMER; HYDROGEN; MONOMER; REPRESSOR PROTEIN; TRYPTOPHAN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DIMERIZATION; ESCHERICHIA COLI; ION EXCHANGE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THEORETICAL STUDY;

ESCHERICHIA COLI;

EID: 33748774141     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.080     Document Type: Article

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