NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY OF MUSSEL ADHESIVE PROTEIN REPEATING PEPTIDE SEGMENT

Citation
Mp. Olivieri et al., NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY OF MUSSEL ADHESIVE PROTEIN REPEATING PEPTIDE SEGMENT, The journal of peptide research, 50(6), 1997, pp. 436-442
Citations number
17
ISSN journal
1397002X
Volume
50
Issue
6
Year of publication
1997
Pages
436 - 442
Database
ISI
SICI code
1397-002X(1997)50:6<436:NSOMAP>2.0.ZU;2-D
Abstract
Mussel adhesive protein (MAP) is the adhesive agent used by the common blue sea mussel (Mytilus edulis) to attach the animal to various unde rwater surfaces. It is generally composed of 75 to 85 repeating decame ric units with the reported primary sequence -Ala(1)-Lys(2)-Pro(3)-Ser (4)-Tyr(5)-Hyp(7)-Thr(8)- DOPA(9)-Lys(10)-COOH. This study examines th is peptide's solution-state conformation using proton nuclear magnetic resonance (NMR) spectroscopy. NMR and molecular modeling of the decam er before and after molecular dynamics calculations in water suggests a conformation that retains an overall bent helix. (C) Munksgaard 1997 .