15N NMR relaxation data reveal significant chemical exchange broadening in the α-domain of human α-lactalbumin

Biochemistry

Volumn 48, Issue 19, 2009, Pages 4031-4039

  Bruylants, Gilles ^a,b   Redfield, Christina ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

BACKBONE DYNAMICS; CALCIUM BINDING PROTEINS; CHEMICAL EXCHANGE; MAGNETIC FIELD STRENGTHS; MODEL FREE; MOLTEN GLOBULE; NATIVE STATE; NATIVE STRUCTURES; NMR RELAXATION; ORDER PARAMETER; STRUCTURAL TRANSITIONS;

AMIDES; CALCIUM; ELECTROMAGNETIC FIELD EFFECTS; MAGNETIC FIELDS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

MAGNETIC DOMAINS;

ALPHA LACTALBUMIN; AMINO ACID; CALCIUM BINDING PROTEIN; DEUTERIUM; HYDROGEN;

ALPHA HELIX; ARTICLE; MAGNETIC FIELD; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; CYSTEINE; DISULFIDES; HUMANS; HYDROGEN-ION CONCENTRATION; LACTALBUMIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

EID: 66049146918     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900023m     Document Type: Article

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