Dimerization of protein G B1 domain at low pH. A conformational switch caused by loss or a single hydrogen bond

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 7, 2010, Pages 1652-1661

  Tomlinson, Jennifer H ^a   Jeremy Craven, C ^a   Williamson, Mike P ^a   Pandya, Maya J ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

strand; Chemical shift; Helix c terminal cap; NMR; Relaxation dispersion; Titration

Indexed keywords

PROTEIN G;

ARTICLE; CONFORMATION; CONTROLLED STUDY; DIMERIZATION; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HYDROGEN BOND; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT;

BACTERIAL PROTEINS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 77951245190     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22683     Document Type: Article

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