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

Nuclear magnetic resonance spectroscopy of mussel adhesive protein repeating peptide segment.
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DOI：
10.1111/j.1399-3011.1997.tb01206.x
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发表时间：
2009-01
期刊：
The journal of peptide research : official journal of the American Peptide Society
影响因子：
--
通讯作者：
M. Olivieri;R. Wollman;J. Alderfer
M. Olivieri;R. Wollman;J. Alderfer
中科院分区：
其他
文献类型：
--
作者：
M. Olivieri;R. Wollman;J. Alderfer

文献摘要

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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.