Article
Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.
Nature communications - 4 Jun 2020
Stephens Amberley D, Zacharopoulou Maria, Moons Rani, Fusco Giuliana, Seetaloo Neeleema, Chiki Anass, Woodhams Philippa J, Mela Ioanna, Lashuel Hilal A, Phillips Jonathan J, De Simone Alfonso, Sobott Frank, Schierle Gabriele S Kaminski
Abstract excerpt
As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but identifying these within the dynamic ensemble of monomeric conformations is difficult. Herein, we used the biologically relevant calcium ion to investigate the conformation of monomeric aSyn in relation to its...
Topics
- Benzothiazoles
- Calcium
- Humans
- Kinetics
- Mutant Proteins
- Mutation
- Phosphorylation
- Protein Aggregates
- Protein Conformation
- Proton Magnetic Resonance Spectroscopy
- Structure-Activity Relationship
- alpha-Synuclein