Time Resolved Fluorescence Spectroscopy

时间分辨荧光光谱是生物化学的有力工具；它可以为大分子复合物的结构和组装提供独特的见解。我们正在利用色氨酸（一种存在于大多数蛋白质中的氨基酸）对由水偶极运动引起的电场的皮秒响应来研究蛋白质附近的水的动力学，这一研究已经进行了十年。Trp的上转换（sub-ps）研究的总体主题由我们在书中单独发表。所有的Trp课程现已转移到上海华东师范大学。

Time-Resolved Fluorescence Spectroscopy is a powerful tool for biochemistry; it can provide unique insights into the structure and assembly of macromolecular complexes. We are wrapping up a decade of studying the dynamics of water near proteins using the picosecond response of Tryptophan(Trp), an amino acid found in most proteins, to the electric field caused by water dipole motions. The overall subject of upconversion (sub-ps) studies of Trp was separately published by us in book chapters. All Trp studies have now moved to East China Normal University in Shanghai. We continued collaborative studies into the status of a primary fuel of heart muscle mitochondria- NADH. Our efforts distinguish free and bound populations of NADH by their different fluorescence lifetimes, and in collaboration with Light Microscopy Core and LCE, we are continually refining 'Decay-Associated Images' software to more rapidly extract profiles of NADH binding within isolated tissue and/or tumor cells. This year we updated DAI software for large images. We continue to develop coupled lifetime and translational diffusion capabilities in time-resolved FCS for this and other projects. We used our spectroscopic tools to help prototype a new imaging molecule for cellular(tissue) oxygen concentration detection- we modified myoglobin to abut a red fluorescent protein tail (e.g. mCherry). They respond to the oxygen-binding of myoglobin by changing lifetime and brightness. We also collaborated on ultrafast studies to aid design and exploitation of fluorescent aptamers, a new window into cellular RNA.