Redesigning the hydrophobic core of a model β-sheet protein: Destabilizing traps through a threading approach

An off‐lattice 46‐bead model of a small all‐β protein has been recently criticized for possessing too many traps and long‐lived intermediates compared with the folding energy landscape predicted for real proteins and models using the principle of minimal frustration. Using a novel sequence design ap...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1999-12, Vol.37 (4), p.582-591
Hauptverfasser:	Sorenson, Jon M., Head-Gordon, Teresa
Format:	Artikel
Sprache:	eng
Schlagworte:	Drug Design Drug Stability Kinetics Models, Molecular multiple histogram method multistate kinetics Mutation off-lattice models protein design Protein Folding Protein Structure, Secondary Proteins - chemistry Proteins - genetics Thermodynamics
Online-Zugang:	Volltext
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