2D IR SPECTROSCOPY OF COLLAGEN DOMAIN STRUCTURES

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. In 1951 Pauling and Corey proposed for the first time a structural configuration for the collagen structure that exhibits a large resemble to the current accepted X-ray diffraction structures for collagen. In this first model the collagen structure was represented by a triple stranded helix stabilized by the hydrogen bonds between strands of polypeptides with alternating cis-trans-amide units, 2 cis- vs. 1 trans-. Today, 28 types of vertebrate collagen structures have been described, which exhibit similar collagen domain structures. NIn spite of much progress on the understanding of the physicochemical characteristics of the structure and stability of collagen domains, there is still a gap in the understanding of the role water molecules and weak hydrogen bond interactions play in these structures. This research project aims to fill up this gap by means of 2D IR spectroscopy.