Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide.

ABSTRACT: The 37-residue human islet amyloid polypeptide (hIAPP or amylin) self-assembles into fibers, the assembly of which has been associated with the disease mechanism of type II diabetes. Infrared spectroscopy in conjunction with isotope labeling is proving to be a powerful tool for studying the aggregation process of hIAPP and other amyloid forming proteins with residue specific structure and kinetic information, but the relationship between the spectroscopic observables and the structure is not fully established. We report a detailed analysis of the linear and 2D IR spectra of hIAPP fibers isotope labeled at seven different residue positions. The features of the 2D IR spectra, including the frequencies, linewidths, intensities, and polarization dependence of the diagonal and cross-peaks, rely

SUBMITTER: Strasfeld DB 

PROVIDER: S-EPMC2901919 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature