Conformation and dynamics of 8-Arg-vasopressin in solution.
Arginine-vasopressin was subjected to a long (11 μs) molecular dynamics simulation in aqueous solution. Analysis of the results by DASH and principal components analyses revealed four main ring conformations that move essentially independently of the faster-moving tail region. Two of these conformations (labeled "saddle") feature well-defined β-turns in the ring and conserved transannular hydrogen bonds, whereas the other two ("open") feature neither. The conformations have been identified and defined and are all of sufficient stability to be considered candidates for biological conformations in their cognate receptors.
Centre for Molecular Design, School of Pharmacy and Biomedical Sciences, University of Portsmouth, Portsmouth, PO1 2DT, UK.
Elke
E
Haensele
Lee
L
Banting
David C
DC
Whitley
Timothy
T
Clark
D000465:Algorithms; D001127:Arginine Vasopressin / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D006860:Hydrogen Bonding; D056004:Molecular Dynamics Simulation; D025341:Principal Component Analysis; D017433:Protein Structure, Secondary; D012995:Solubility; D013329:Structure-Activity Relationship
D004220:Disulfides; D001127:Arginine Vasopressin