Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics.

ABSTRACT: The genetic missense A30P mutation of the wild-type α-synuclein protein results in the replacement of the 30th amino acid residue from alanine (Ala) to proline (Pro) and was initially found in the members of a German family who developed Parkinson's disease. Even though the structures of these proteins have been measured before, detailed understanding about the structures and their relationships with free energy landscapes is lacking, which is of interest to provide insights into the pathogenic mechanism of Parkinson's disease. We report the secondary and tertiary structures and conformational free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins in an aqueous solution environment via extensive parallel tempering molecular dynamics simulations along with thermod

SUBMITTER: Wise-Scira O 

PROVIDER: S-EPMC3607329 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature