Nuclear magnetic resonance spectroscopy of mussel adhesive protein repeating peptide segment

Nuclear magnetic resonance spectroscopy of mussel adhesive protein repeating peptide segment

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)‐Lys(2)‐Pro(3)‐Ser(4)‐Tyr(5)‐Hyp(6)...

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Veröffentlicht in:The journal of peptide research 1997-12, Vol.50 (6), p.436-442
Hauptverfasser: OLIVIERI, MARION P., WOLLMAN, ROBERT M., ALDERFER, JAMES L.
Format: Artikel
Sprache:eng
Schlagworte:
Adhesives - chemistry
Amino Acid Sequence
Amino Acids - analysis
Bioadhesives
Chemical Phenomena
Chemistry, Physical
Chromatography, High Pressure Liquid
Hydrogen Bonding
Hydroxyproline - chemistry
Levodopa - chemistry
Magnetic Resonance Spectroscopy
Molecular Structure
mussel adhesive protein
nuclear magnetic resonance
peptides
Protein Conformation
Protein Structure, Secondary
Proteins - chemistry
Repetitive Sequences, Nucleic Acid
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Zusammenfassung: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)‐Lys(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. © Munksgaard 1997.
ISSN:1397-002X
1399-3011
DOI:10.1111/j.1399-3011.1997.tb01206.x