The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings

Journal of Molecular Biology

Volumn 329, Issue 3, 2003, Pages 551-563

  Millet, Oscar ^a   Mittermaier, Anthony ^a   Baker, David ^b   Kay, Lewis E ^a  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Deuterium relaxation; Protein stability; Side chain dynamics; Site directed mutagenesis

Indexed keywords

METHYL GROUP; PROTEIN; PROTEIN A20V; PROTEIN F22L; PROTEIN L; TRITIUM; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ANALYTICAL PARAMETERS; ARTICLE; CHEMICAL BOND; DYNAMICS; ENERGY; MOTION; MUTATION; NUCLEAR MAGNETIC RESONANCE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN VARIANT; SCALAR COUPLING; STRUCTURE ANALYSIS; TIME; X RAY ANALYSIS;

EID: 0038630482     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00471-6     Document Type: Article

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