Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable β-hairpin: Atomic details of trimer dissociation and local β-hairpin stability from residual dipolar couplings

Journal of Molecular Biology

Volumn 344, Issue 4, 2004, Pages 1051-1069

  Meier, Sebastian ^a   Güthe, Sarah ^a   Kiefhaber, Thomas ^a   Grzesiek, Stephan ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

NMR spectroscopy; order parameter; protein folding; structure; thermodynamics

Indexed keywords

ALCOHOL; AMINO ACID DERIVATIVE; FOLDON; MONOMER; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG; WATER;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISSOCIATION; HIGH TEMPERATURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; STRUCTURE ANALYSIS; THERMOSTABILITY;

EID: 8544254692     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.079     Document Type: Article

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