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 ϕ, ψ, χ1 dihedral angles, is proposed to approach the formation at the atom level of both principal elements of protein secondary structure, the α‐helix and the β‐hairpin structures. Expecting to understand wh...

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Veröffentlicht in:	Journal of peptide science 2006-01, Vol.12 (1), p.33-42
Hauptverfasser:	Busetta, Bernard, Picard, Philippe, Précigoux, Gilles
Format:	Artikel
Sprache:	eng
Schlagworte:	Computer Simulation folding simulation implicit solvent representation Magnetic Resonance Spectroscopy - methods Magnetic Resonance Spectroscopy - standards Oligopeptides - chemistry Protein Conformation Protein Folding Protein Structure, Secondary Reference Standards
Online-Zugang:	Volltext
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