The pH dependence of CD2 domain 1 self-association and 15N chemical exchange broadening is correlated with the anomalous pKa of Glu41+

Biochemistry

Volumn 41, Issue 50, 2002, Pages 14680-14688

  Chen, H A ^a,d   Pfuhl, Mark ^a,c   Driscoll, Paul C ^a,b  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b LUDWIG INSTITUTE FOR CANCER RESEARCH   (United Kingdom)

^c UNIVERSITY OF LEICESTER   (United Kingdom)

^d IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOLOGY; MUTAGENESIS; PH EFFECTS; PROTEINS; RESONANCE;

NUCLEAR RELAXATION MEASUREMENTS;

BIOCHEMISTRY;

CD2 ANTIGEN; GLUTAMINE; IMMUNOGLOBULIN; NITROGEN 15;

ARTICLE; BINDING AFFINITY; CONCENTRATION RESPONSE; CRYSTAL STRUCTURE; ION EXCHANGE; MUTAGENESIS; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTON TRANSPORT; SEQUENCE HOMOLOGY;

AMINO ACID SUBSTITUTION; ANIMALS; ANTIGENS, CD2; CARBON ISOTOPES; CELL ADHESION; DIMERIZATION; GLUTAMIC ACID; GLUTAMINE; HYDROGEN-ION CONCENTRATION; MODELS, CHEMICAL; MODELS, MOLECULAR; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, TERTIARY; RATS; THERMODYNAMICS;

EID: 0037126727     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026447x     Document Type: Article

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