By Topic

Structural Character of Protein Complex a-syn12 Peptide and Synphilin-1 Studied Using Molecular Dynamics Simulation

Sign In

Cookies must be enabled to login.After enabling cookies , please use refresh or reload or ctrl+f5 on the browser for the login options.

Formats Non-Member Member
$33 $13
Learn how you can qualify for the best price for this item!
Become an IEEE Member or Subscribe to
IEEE Xplore for exclusive pricing!
close button

puzzle piece

IEEE membership options for an individual and IEEE Xplore subscriptions for an organization offer the most affordable access to essential journal articles, conference papers, standards, eBooks, and eLearning courses.

Learn more about:

IEEE membership

IEEE Xplore subscriptions

1 Author(s)
Liling Zhao ; Key Lab. of Biophys. in Univs. of Shandong, Dezhou Univ., Dezhou, China

Molecular dynamics simulations method was used to study the dynamics and structural character of α-syn12 peptide complex with synphilin-1 protein in aqueous solution at low pH by using GROMOS 43A1 force field. The α-syn12 peptide aggregates faster at low pH than at neutral pH.

Published in:

Modeling, Simulation and Visualization Methods (WMSVM), 2010 Second International Conference on

Date of Conference:

15-16 May 2010