Coarse-grain simulations of the R-SNARE fusion protein in its membrane environment detect long-lived conformational sub-states.

Journal article

Coarse-grain molecular dynamics are used to look at conformational and dynamic aspects of an R-SNARE peptide inserted in a lipid bilayer. This approach allows carrying out microsecond-scale simulations which bring to light long-lived conformational sub-states potentially interesting in the context of the membrane fusion mechanism mediated by the SNARE proteins. We show that these coarse-grain models are in agreement with most experimental data on the SNARE system, but differ in some details that may have a functional interest, most notably in the orientation of the soluble part of R-SNARE that does not appear to be spontaneously accessible for SNARE complex formation. We also compare rat and yeast sequences of R-SNARE and find some minor differences in their behavior.

Authors: Durrieu, M; Bond, P; Sansom, MS; Lavery, R; Baaden, M

• Journal: Chemphyschem : a European journal of chemical physics and physical chemistry
• Volume: 10
• Issue: 9-10
• Pages: 1548-1552
• Publication date: 2009-07-01
• DOI: 10.1002/cphc.200900216
• EISSN: 1439-7641
• ISSN: 1439-4235
• Language: English
• Keywords: Protein Conformation; Cell Membrane; Animals; Amino Acid Sequence; SNARE Proteins; Recombinant Fusion Proteins; Rats; Lipid Bilayers; Molecular Sequence Data