Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner

“…Intra-and intermolecular contacts can be detected in monomeric, unfolded αS and are implicated in modulating the aggregation propensity (Bertoncini et al, 2005;Dedmon et al, 2005;Outeiro et al, 2008;Wu and Baum, 2010). The negatively charged C-terminus remains disordered in several conformational states such as monomeric, fibrillar and membrane-bound αS (Del Mar et al, 2005;Eliezer et al, 2001;Qin et al, 2007;Ulmer et al, 2005;Vilar et al, 2008). In Lewy õbodies, 90% of αS is estimated to be phosphorylated at S129 in the C-terminus (Fujiwara et al, 2002).…”

19F NMR studies of α‐synuclein‐membrane interactions

“…1) is a 140 amino-acid, intrinsically-disordered protein associated with Parkinson's disease and other neurodegenerative disorders [1][2][3][4][5][6][7][8] whose function is hypothesized to involve its interaction with membranes. [8][9][10][11][12] The protein binds lipids and anionic detergents through the seven imperfect, cationic, 11-amino acid repeats located in its N-terminal and hydrophobic regions.…”

“…[8][9][10][11][12] The protein binds lipids and anionic detergents through the seven imperfect, cationic, 11-amino acid repeats located in its N-terminal and hydrophobic regions. [6][7][8][13][14][15][16][17][18][19][20] Electron paramagnetic resonance (EPR) data on its complex with small unilamellar vesicles (SUVs) suggest that the first $100 residues of the monomeric protein adopt an a-helical conformation that lies on the membrane surface. [21][22][23][24][25] The last $40 residues lack defined structure and do not appear to be involved in membrane interactions.…”

Protein-metal interactions of calmodulin and α-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry

“…␣-Synuclein is a natively disordered protein and adopts a wide distribution of conformations [24]. Commonly used techniques to determine protein structure, such as X-ray crystallography, are inappropriate for disordered proteins like ␣-synuclein.…”