Journal Article

PreJuSER-54183

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Folding of proteins with diverse folds

Mohanty, S.FZJ* ; Hansmann, U. H. E.FZJ*

2006
Rockefeller Univ. Press New York, NY

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Please use a persistent id in citations: http://hdl.handle.net/2128/2373  doi:10.1529/biophysj.106.087668

Abstract: Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure.

Keyword(s): Computer Simulation (MeSH) ; Models, Chemical (MeSH) ; Models, Molecular (MeSH) ; Models, Statistical (MeSH) ; Protein Conformation (MeSH) ; Protein Folding (MeSH) ; Proteins: chemistry (MeSH) ; Proteins: ultrastructure (MeSH) ; Proteins ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. John von Neumann - Institut für Computing (NIC)

Research Program(s):

1. Scientific Computing (P41)

Appears in the scientific report 2006
Notes: This version is available at the following Publisher URL: http://www.biophysj.org/

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