The conformation of dehydroalanine in short homopeptides: molecular dynamics simulations of a 6-residue chain.
A molecular dynamics study about the conformational preferences in a chloroform solution of a homo-oligomer constituted by six residues of dehydroalanine is presented. For this purpose, two sets of force-field parameters and explicit solvent molecules have been used. Furthermore, ab initio calculations have been performed in order to estimate 1[H]-NMR chemical shifts. Results have been compared with experimental data.
Departament d'Enginyeria Quimica, ETSEIB, Universitat Politècnica de Catalunya, Diagonal 647, E-08028, Barcelona, Spain.
David
D
Zanuy
Jordi
J
Casanovas
Carlos
C
Alemán
D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry*; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D011789:Quantum Theory; D013816:Thermodynamics
D009842:Oligopeptides; C015102:dehydroalanine; D000409:Alanine