FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding.

ABSTRACT: X-ray crystallography of collagen model peptides has provided high-resolution structures of the basic triple-helical conformation and its water-mediated hydration network. Vibrational spectroscopy provides a useful bridge for transferring the structural information from X-ray diffraction to collagen in its native environment. The vibrational mode most useful for this purpose is the amide I mode (mostly peptide bond C=O stretch) near 1650 cm-1. The current study refines and extends the range of utility of a novel simulation method that accurately predicts the infrared (IR) amide I spectral contour from the three-dimensional structure of a protein or peptide. The approach is demonstrated through accurate simulation of the experimental amide I contour in solution for both a standard triple he

SUBMITTER: Bryan MA 

PROVIDER: S-EPMC2570338 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature