Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties.

ABSTRACT: N-Terminal acetylation of α-synuclein (aS), a protein implicated in the etiology of Parkinson's disease, is common in mammals. The impact of this modification on the protein's structure and dynamics in free solution and on its membrane binding properties has been evaluated by high-resolution nuclear magnetic resonance and circular dichroism (CD) spectroscopy. While no tetrameric form of acetylated aS could be isolated, N-terminal acetylation resulted in chemical shift perturbations of the first 12 residues of the protein that progressively decreased with the distance from the N-terminus. The directions of the chemical shift changes and small changes in backbone (3)J(HH) couplings are consistent with an increase in the α-helicity of the first six residues of aS, although a high degree of dy

SUBMITTER: Maltsev AS 

PROVIDER: S-EPMC3383124 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature