Volume 35, Number 8, September II 1996
|Page(s)||627 - 632|
|Section||Cross-disciplinary physics and related areas of science and technology|
|Published online||01 September 2002|
A criterion that determines fast folding of proteins: A model study
Física, P. Universidad Católica de Chile - Casilla 306, Santiago
2 Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA
Accepted: 23 July 1996
We consider the statistical mechanics of a full set of two-dimensional protein-like heteropolymers, whose thermodynamics is characterized by the coil-to-globular () and the folding (Tf) transition temperatures. For our model, the typical time scale for reaching the unique native conformation is shown to scale as . We argue that Tf scales linearly with the inverse of entropy of low-energy non-native states, whereas is almost independent of it. As , non-productive intermediates decrease, and the initial rapid collapse of the protein leads to structures resembling the native state. Based solely on thermodynamic information, σ can be used to predict sequences that fold rapidly.
PACS: 87.10.+e – General, theoretical, and mathematical biophysics (including logic of biosystems, quantum biology, and relevant aspects of thermodynamics, information theory, cybernetics, and bionics) / 05.70.Fh – Phase transitions: general aspects / 64.60.Cn – Order-disorder and statistical mechanics of model systems
© EDP Sciences, 1996
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