Stability of protein-bound conformations of bioactive peptides: The folded conformation of an epidermal growth factor-like thrombomodulin fragment is similar to that recognized by thrombin

Biopolymers

Volumn 65, Issue 6, 2002, Pages 373-386

  Song, Jianxing ^a   Xu, Ping ^a   Koutychenko, Anatol ^a   Ni, Feng ^a  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

Bioactive peptides; Conformational stability; Epidermal growth factor like sub domain; NMR; Thrombin; Thrombomodulin

Indexed keywords

BIOACTIVE PEPTIDES;

CHEMICAL BONDS; CONFORMATIONS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PH EFFECTS; TOPOLOGY;

PROTEINS;

EPIDERMAL GROWTH FACTOR; PEPTIDE FRAGMENT; PROTEIN; THROMBIN; THROMBIN INHIBITOR; THROMBOMODULIN;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; DISULFIDE BOND; HYDROPHOBICITY; MODEL; MOLECULAR RECOGNITION; PH; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; STRUCTURAL HOMOLOGY; TEMPERATURE; TOPOGRAPHY;

MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; THROMBIN; THROMBOMODULIN;

EID: 0037114707     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10253     Document Type: Article

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