报告题目： Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET
报 告 人：William Zagotta, professor, University of Washington
主 持 人：Pro. Huaiyu Yang
报告时间：2023年10月13日 9:30-10:30
报告地点：闵行校区生命科学学院534小会议室
报告人简介：
William Zagotta got his PhD in Stanford University. He worked in HHMI and University of Washington since the 1990s. He is mainly focused on studying the opening and closing conformational changes in Ion channels by using a combination of molecular biology and patch-clamp techniques. His works were published on Science, Nature, Neron and PNAS et. al. The H-index is round 50.
报告内容：
Protein allostery plays a pivotal role in the regulation of virtually all biological processes including enzymatic catalysis, signal transduction, gene regulation, and cellular motility. The mechanism of allostery involves an intricate choreography of the protein’s structure and energetics. While we now have many static pictures of the protein structure, measurements of protein energetics and dynamics are more difficult and are key to understanding protein function. Over the last decade we have developed novel methods for measuring protein energetics and dynamics using transition metal ion FRET (tmFRET). Here we expand the utility of tmFRET to measure conformational changes across a broader range of distances using metals bound to bipyridyl derivatives as FRET acceptors. Using a model protein (maltose binding protein, MBP) and a cyclic nucleotide-binding domain of an ion channel (SthK), we show that time-resolved tmFRET can quantify both the heterogeneity of any given conformational state and the energetics that govern the distribution of a protein among conformational states, collectively known as protein dynamics.
