title: Structural studies of amyloids by quenched hydrogen-deuterium exchange by NMR.
abstract: The elucidation of the structure of amyloid fibrils and related aggregates is an important step towards understanding the pathogenesis of diseases such as Alzheimer's and Parkinson's, which feature protein misfolding and/or aggregation. However, the large size and poor solubility of amyloid-like fibrils make them resistant to high-resolution structure determination. Here, we describe the use of hydrogen-deuterium exchange coupled with NMR as an indirect strategy to determine the folding regions of amyloid-forming proteins at residue level resolution.
authors.affiliation: Neurodegeneration Unit, Centro Nacional de Microbiología, Instituto de Salud Carlos III, Madrid, Spain. mvilar@isciii.es
authors.forename: Marçal
authors.initials: M
authors.lastname: Vilar
authors.forename: Lei
authors.initials: L
authors.lastname: Wang
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D041961:Deuterium Exchange Measurement / Q000379:methods*; D004121:Dimethyl Sulfoxide / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D012995:Solubility
chemical_list: D000682:Amyloid; D004121:Dimethyl Sulfoxide