STUDY OF THE MOLECULAR BASIS OF BLOOD CLOT EXTENSIBILITY BY FTIR

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 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 研究中心，而研究中心不一定是研究者所在的机构。 由纤维蛋白（血凝块中的主要蛋白质）形成的纤维是已知的最可延展的生物聚合物，但这种延展性的分子基础尚未被探索。我们想使用定制的血块拉伸器拉伸夹在IR透明窗口之间的定向血块，以通过使用FTIR光谱仪监测酰胺I带来解决这个问题。我们希望在环境条件下首次观察到二级结构的变化，特别是血液凝块中潜在的α-螺旋到β-折叠或无规卷曲的转变。

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. Fibers formed from fibrin (the primary protein in blood clots) are the most extensible biological polymers known, but the molecular basis for this extensibility has not been explored. We would like to use a custom-made clot stretcher to stretch oriented clots sandwiched between IR transparent windows to address this question by monitoring the amide I band using an FTIR spectrometer. We hope to observe secondary structural changes, specifically a potential alpha-helix to beta-sheet or random coil transition in blood clots for the first time under ambient conditions.