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Nuclear magnetic resonance spectroscopy of mussel adhesive protein repeating peptide segment.

作者信息

Olivieri M P, Wollman R M, Alderfer J L

机构信息

Division of Mathematics and Natural Sciences, D'Youville College, Buffalo, New York, USA.

出版信息

J Pept Res. 1997 Dec;50(6):436-42. doi: 10.1111/j.1399-3011.1997.tb01206.x.

DOI:10.1111/j.1399-3011.1997.tb01206.x
PMID:9440044
Abstract

Mussel adhesive protein (MAP) is the adhesive agent used by the common blue sea mussel (Mytilus edulis) to attach the animal to various underwater surfaces. It is generally composed of 75 to 85 repeating decameric units with the reported primary sequence NH2-Ala(1)-Lyst(2)-Pro(3)-Ser(4)-Tyr(5)-Hyp(6)-Hyp(7)-Thr(8)-DOPA( 9)- Lys(10)-COOH. This study examines this peptide's solution-state conformation using proton nuclear magnetic resonance (NMR) spectroscopy. NMR and molecular modeling of the decamer before and after molecular dynamics calculations in water suggests a conformation that retains an overall bent helix.

摘要

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