How protein structures can mislead protein engineers

发布时间 :2017-05-16  阅读次数 :1424

报告题目:How protein structures can mislead protein engineers

报  告 人:Romas Kazlauskas教授,University of Minnesota, USA

报告时间:5月18日(星期四) 13:30

报告地点:闵行校区生物药学楼2-116会议室

联  系 人:杨广宇 yanggy@sjtu.edu.cn
 

Abstract

       Rapid advances in structural biology and computer modeling make protein structures powerful images. While these structures are important starting points for protein engineering, they mislead when protein engineers forget about features that protein structure cannot show. This lecture will describe two examples where protein structures tell only part of the story: engineering more stable proteins and engineering new catalytic activity. In engineering more stable proteins, researchers often focus on strengthening interactions between amino acids in the folded form, but forget that the unfolded form, whose structure is unknown, is an equally important contributor to protein stability. I will describe an easy approach to protein stabilization using the consensus sequence approach. In engineering new catalytic activity, researchers focus on the new activity, ignoring the possibility that the path to the new actvity may be indirect. I will describe the evolution of an esterase to a hydroxynitrile lyase where ancestral enzymes may have used an alternative extinct mechanism.

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