PROTEIN CONFORMATIONAL CHANGE TRIGGERED BY NI-BCHL-A EXCITATION

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。我们计划研究Ni-BChl-a加入到de-novo模型中光激发后的结构变化和动力学机制。因此，模型是一种纯粹的合成肽结构，具有蛋白质的灵活性，可以在分子水平上进行定制，以完成天然蛋白质所显示的各种各样的化学、机械和电子功能，但具有生物物质所不具备的简单性和稳健性。从以往对Ni-BChl-a配合物的光谱学研究可知，光激发后轴向配体发生排斥。我们希望利用这种光触发器来启动de-novo蛋白质中的蛋白质运动，以研究蛋白质的构象动力学。超快瞬态吸收光谱将用于进一步研究光激发后发生的结构变化。

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. We plan to study structural changes and kinetic mechanism after photoexcitation of a Ni-BChl-a incorporated into a de-novo maquette. A maquette is thereby a purely synthetic peptide structures with protein flexibility that is tailored at the molecular level to accomplish as wide a variety of chemical, mechanical and electrical functions as displayed by natural proteins, but with a simplicity and robustness uncharacteristic of living matter. From previous studies on the optical spectroscopy of Ni-BChl-a complexes, it is known that a repulsion of the axial ligands occurs after photoexcitation. We would like to use this phototrigger to initiate protein motion in a de-novo protein to study protein conformational dynamics. Ultrafast transient absorption spectroscopy is to be used to further investigate into structural changes occurring after photoexcitation.