title: Deep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation.
abstract: Deep UV resonance Raman spectroscopy is a powerful technique for probing the structure and formation mechanism of protein fibrils, which are traditionally difficult to study with other techniques owing to their low solubility and noncrystalline arrangement. Utilizing a tunable deep UV Raman system allows for selective enhancement of different chromophores in protein fibrils, which provides detailed information on different aspects of the fibrils' structure and formation. Additional information can be extracted with the use of advanced data treatment such as chemometrics and 2D correlation spectroscopy. In this chapter we give an overview of several techniques for utilizing deep UV resonance Raman spectroscopy to study the structure and mechanism of formation of protein fibrils. Clever use of hydrogen-deuterium exchange can elucidate the structure of the fibril core. Selective enhancement of aromatic amino acid side chains provides information about the local environment and protein tertiary structure. The mechanism of protein fibril formation can be investigated with kinetic experiments and advanced chemometrics.
authors.affiliation: Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY, 12222, USA.
authors.forename: Joseph D
authors.initials: JD
authors.lastname: Handen
authors.affiliation: Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY, 12222, USA. ilednev@albany.edu.
authors.forename: Igor K
authors.initials: IK
authors.lastname: Lednev
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000682:Amyloid / Q000737:chemistry* / Q000235:genetics; D066263:Protein Aggregation, Pathological / Q000235:genetics*; D011487:Protein Conformation; D017510:Protein Folding; D013059:Spectrum Analysis, Raman / Q000379:methods*; D014466:Ultraviolet Rays
chemical_list: D000682:Amyloid
keywords: 2DCoS; Chemometrics; Fibrils; Hydrogen-deuterium exchange; Protein (un)folding kinetics; Protein folding; UV resonance Raman spectroscopy