2D IR SPECTROSCOPY OF COLLAGEN DOMAIN STRUCTURES

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 1951年，Pauling和Corey首次提出了一种胶原蛋白结构的结构构型，这种结构与目前公认的胶原蛋白X射线衍射结构非常相似。在第一个模型中，胶原结构由一个三链螺旋结构表示，由具有交替顺式-反式酰胺单元的多肽链之间的氢键稳定，2个顺式-对1个反式-。今天，已经描述了28种脊椎动物胶原结构，它们表现出类似的胶原域结构。尽管对胶原域的结构和稳定性的物理化学特征的了解已经取得了很大的进展，但对水分子和弱氢键相互作用在这些结构中所起的作用的理解仍然存在差距。本研究项目旨在通过二维红外光谱分析来填补这一空白。

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.