2D IR SPECTROSCOPY OF COLLAGEN DOMAIN STRUCTURES

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 中心，但不一定是研究者所在的机构。 1951年，Pauling和Corey首次提出了胶原蛋白结构的结构构型，该构型与目前公认的胶原蛋白的X射线衍射结构非常相似。 在该第一模型中，胶原蛋白结构由三链螺旋表示，该三链螺旋由具有交替的顺式-反式-酰胺单元（2顺式-对1反式-）的多肽链之间的氢键稳定。 今天，已经描述了28种脊椎动物胶原结构，它们表现出相似的胶原结构域结构。 尽管对胶原结构域的结构和稳定性的物理化学特征的理解取得了很大进展，但对水分子和弱氢键相互作用在这些结构中的作用的理解仍然存在差距。 该研究项目旨在通过二维红外光谱来填补这一空白。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 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.