Glutamine Side Chain ¹³C═¹⁸O as a Nonperturbative IR Probe of Amyloid Fibril Hydration and Assembly.

ABSTRACT: Infrared (IR) spectroscopy has provided considerable insight into the structures, dynamics, and formation mechanisms of amyloid fibrils. IR probes, such as main chain ¹³C═¹⁸O, have been widely employed to obtain site-specific structural information, yet only secondary structures and strand-to-strand arrangements can be probed. Very few nonperturbative IR probes are available to report on the side-chain conformation and environments, which are critical to determining sheet-to-sheet arrangements in steric zippers within amyloids. Polar residues, such as glutamine, contribute significantly to the stability of amyloids and thus are frequently found in core regions of amyloid peptides/proteins. Furthermore, polyglutamine (polyQ) repeats form toxic aggregates in several neu

SUBMITTER: Wu H 

PROVIDER: S-EPMC6800148 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature