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FEBS Letters

Volumn 493, Issue 2-3, 2001, Pages 70-74

The solution structure of the disulphide-linked homodimer of the human trefoil protein TFF1

(4) Williams, Mark A a,c Westley, Bruce R b May, Felicity E B b Feeney, James a

a NATIONAL INSTITUTE FOR MEDICAL RESEARCH (United Kingdom)

b NEWCASTLE UNIVERSITY (United Kingdom)

c UNIVERSITY COLLEGE LONDON (United Kingdom)

Author keywords

Nuclear magnetic resonance; Solution structure; TFF1; TFF1 dimer; Trefoil factor family

Indexed keywords

DIMER; DISULFIDE; ISOPROTEIN; TREFOIL PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; DISULFIDE BOND; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; CALCIUM; CYSTEINE; DIMERIZATION; DISULFIDES; GROWTH SUBSTANCES; HUMANS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUCINS; MUSCLE PROTEINS; NEUROPEPTIDES; OSMOLAR CONCENTRATION; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEINS; SOLUTIONS; TUMOR SUPPRESSOR PROTEINS;

LOTUS;

EID: 0035970760 PISSN: 00145793 EISSN: None Source Type: Journal
DOI: 10.1016/S0014-5793(01)02276-1 Document Type: Article

Times cited : (44)

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