Computer simulations of de novo designed helical proteins

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Title: Computer simulations of de novo designed helical proteins
Author: Sikorski, Andrzej ; Kolinski, Andrzej ; Skolnick, Jeffrey
Abstract: In the context of reduced protein models, Monte Carlo simulations of three de novo designed helical proteins (four-member helical bundle) were performed. At low temperatures, for all proteins under consideration, protein-like folds having different topologies were obtained from random starting conformations. These simulations are consistent with experimental evidence indicating that these de novo designed proteins have the features of a molten globule state. The results of Monte Carlo simulations suggest that these molecules adopt four-helix bundle topologies. They also give insight into the possible mechanism of folding and association, which occurs in these simulations by on-site assembly of the helices. The low-temperature conformations of all three sequences have the features of a molten globule state.
Description: © 1998 by the Biophysical Society
Type: Article
URI: http://hdl.handle.net/1853/41942
ISSN: 0006-3495
Citation: Sikorski, A, Kolinski A, Skolnick J. 1998. Computer simulations of de novo designed helical proteins. Biophysical journal. 75(1):92-105.
Date: 1998-07
Contributor: Uniwersytet Warszawski. Wydział Chemii
Scripps Research Institute. Dept. of Molecular Biology
Publisher: Georgia Institute of Technology
Biophysical Society
Subject: Globular proteins
Monte Carlo method
Protein folding
Simulation

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