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Volumn 39, Issue 51, 2000, Pages 15742-15756

Characterization of the EGF-like module pair 3-4 from vitamin K-dependent protein S using NMR spectroscopy reveals dynamics on three separate time scales and extensive effects from calcium binding

(5) Muranyi, A a Evenas J a,b Stenberg, Y a,c Stenflo, J a Drakenberg, T a

a LUND UNIVERSITY (Sweden)

b UNIVERSITY OF TORONTO (Canada)

c BioInvent International AB (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; ANTICOAGULANT AGENT; CALCIUM; EPIDERMAL GROWTH FACTOR; LYSINE; PROLINE; PROTEIN S; VITAMIN K GROUP;

ANISOTROPY; ARTICLE; CALCIUM BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN POLYMORPHISM; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANISOTROPY; BINDING SITES; CALCIUM; CALCIUM-BINDING PROTEINS; EPIDERMAL GROWTH FACTOR; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN S; THERMODYNAMICS; TITRIMETRY;

EID: 0034719161 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0004450 Document Type: Article

Times cited : (10)

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