Journal Article

PreJuSER-59988

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Folding of a Miniprotein with mixed Fold

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

2007
American Institute of Physics Melville, NY

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Please use a persistent id in citations: http://hdl.handle.net/2128/19080  doi:10.1063/1.2753835

Abstract: Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of beta sheets. Our analysis of the observed folding events suggests that the C-terminal helix of FSD-EY is much more stable than the N-terminal beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix.

Keyword(s): DNA-Binding Proteins: chemistry (MeSH) ; Hydrophobic and Hydrophilic Interactions (MeSH) ; Models, Molecular (MeSH) ; Protein Folding (MeSH) ; Protein Structure, Secondary (MeSH) ; Thermodynamics (MeSH) ; Transcription Factors: chemistry (MeSH) ; DNA-Binding Proteins ; FSD-1 protein, synthetic ; Transcription Factors ; 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 2007

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Database coverage:

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