Transmembrane Helices Have Rough Energy Surfaces

The folding and function of proteins is guided by their multidimensional energy landscapes. Local corrugations on rugged energy surfaces determine the dynamics of functionally related conformational changes and molecular flexibilities. By varying the temperature during the force-induced unfolding of...

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Veröffentlicht in:	Journal of the American Chemical Society 2007-01, Vol.129 (2), p.246-247
Hauptverfasser:	Janovjak, Harald, Knaus, Helene, Muller, Daniel J
Format:	Artikel
Sprache:	eng
Schlagworte:	Membranes, Artificial Microscopy, Atomic Force Models, Molecular Protein Conformation Protein Folding Protein Structure, Secondary Surface Properties Thermodynamics
Online-Zugang:	Volltext
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