Simulation of oligopeptide dynamics and folding. The use of NMR chemical shifts to analyse the MD trajectories.
In this paper, a simulation of the folding process, based on a random perturbations of the phi, psi, chi1 dihedral angles, is proposed to approach the formation at the atom level of both principal elements of protein secondary structure, the alpha-helix and the beta-hairpin structures. Expecting to understand what may happen in solution during the formation of such structures, the behaviour of large sets of random conformations that are generated for small oligopeptides was analysed. Different factors that may influence the folding (as conformational propensity, hydrophobic interactions and side-chain mobility) were investigated. The difference between the corresponding theoretical folding and the real conformational diversity that is observed in solution is appraised by a comparison between the calculated and observed NMR secondary chemical shifts. From this study it appears that hydrophobic interactions and mobility represent the principal factors that initiate folding and determine the observed hydrogen-bond pattern, which subsequently allows packing between the peptide side chains.
Busetta
Bernard
B
Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, 33405 Talence, France.
Picard
Philippe
P
Précigoux
Gilles
G
D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards*; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012015:Reference Standards
D009842:Oligopeptides