Common Folding Mechanism of a β-Hairpin Peptide via Non-native Turn Formation Revealed by Unbiased Molecular Dynamics Simulations.

The folding of a 15-residue β-hairpin peptide (Peptide 1) is characterized using multiple unbiased, atomistic molecular dynamics (MD) simulations. Fifteen independent MD trajectories, each 2.5 μs-long for a total of 37.5 μs, are performed of the peptide in explicit solvent, at room temperature, and...

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Publicado en:	Journal of the American Chemical Society Vol. 131; no. 50; pp. 18147 - 18153
Autores principales:	Thukral, Lipi, Smith, Jeremy C., Daidone, Isabella
Formato:	Artículo
Publicado:	American Chemical Society 12/23/2009
Materias:	Molecular dynamics Peptides Quantum trajectories Chemical research Sampling (Process)
Acceso en línea:	Ver este registro en EBSCOhost