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)-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.
Olivieri
M P
MP
Division of Mathematics and Natural Sciences, D'Youville College, Buffalo, New York, USA. mpo@koolnet.org
Wollman
R M
RM
Alderfer
J L
JL
D000269:Adhesives / Q000737:chemistry*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002851:Chromatography, High Pressure Liquid; D006860:Hydrogen Bonding; D006909:Hydroxyproline / Q000737:chemistry; D007980:Levodopa / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012091:Repetitive Sequences, Nucleic Acid
D000269:Adhesives; D000596:Amino Acids; D011506:Proteins; C037403:adhesive protein, mussel; D007980:Levodopa; D006909:Hydroxyproline