Folding behavior of model proteins with weak energetic frustration

The native structure of fast-folding proteins, albeit a deep local free-energy minimum, may involve a relatively small energetic penalty due to nonoptimal, though favorable, contacts between amino acid residues. The weak energetic frustration that such contacts represent varies among different prote...

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Veröffentlicht in:	The Journal of chemical physics 2004-06, Vol.120 (23), p.11292-11303
Hauptverfasser:	Locker, C Rebecca, Hernandez, Rigoberto
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Computer Simulation Energy Transfer Models, Chemical Models, Molecular Molecular Sequence Data Motion Protein Conformation Protein Folding Proteins - chemistry Proteins - ultrastructure Sequence Analysis, Protein - methods
Online-Zugang:	Volltext
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