Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds

Biochemistry

Volumn 44, Issue 43, 2005, Pages 14055-14061

  He, Yanan ^a   Yeh, Deok Cheon ^a   Alexander, Patrick ^a   Bryan, Philip N ^a   Orban, John ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGES; CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; STRUCTURE (COMPOSITION);

CONFORMATIONAL SWITCHING; IGG BINDING DOMAINS; PHAGE DISPLAY; THREE-DIMENSIONAL STRUCTURES;

PROTEINS;

IMMUNOGLOBULIN G; PROTEIN A; PROTEIN G;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA CHAIN; BINDING SITE; CONFORMATIONAL TRANSITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; IMMUNOGLOBULIN G; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MUTATION; NERVE TISSUE PROTEINS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STAPHYLOCOCCAL PROTEIN A; THERMODYNAMICS;

EID: 27444443861     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051232j     Document Type: Article

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