报告题目：Advances of Structural Membrane Proteomics and Its Applications

报告人：Guohong Peng 博士（德国马普生物物理研究所）

主持人：邵宁副研究员

时间：2014年3月31日（星期一）  14:30-16:00

地点：综合实验楼第二会议室

报告人简介： Dr. Guohong Peng

Group Leader at the Department of Molecular Membrane Biology  (Director, Prof. Dr. Dr. hc. Hartmut Michel), Max Planck Institute of Biophysics since 2004

Website: http://www.biophys.mpg.de/en/institute/molecular-membrane-biology/projects-and-research-groups/structural-membrane-proteomics.html

Research Interests

Proteins from hyperthermophilic organisms are considered to be more stable and more rigid than their mesophilic counterparts. Therefore, the chance to obtain stable, homogeneous and crystallizable membrane protein complexes from (hyper)thermophilic organisms should be better than with complexes from mesophilic ones.  Aquifex aeolicus is a hyperthermophilic eubacterium. It grows up to 95 oC. The complete genome of A. aeolicus was sequenced. Two pronounced features characterize A. aeolicus genome. We purify and characterize as many proteins/protein complexes from overproduction and native membranes of A. aeolicus as possible using conventional biochemical techniques. The proteins are identified by mass spectrometry, subjected to crystallization trials, and functionally characterized by enzymatic assays, spectroscopic and electrophysiological techniques.

So far we have identified 140 proteins which belong to 99 membrane proteins/protein complexes. These are primarily involved in metabolism and energy transduction. 22 transport proteins have been found. 16 membrane proteins/membrane protein complexes could be isolated and identified, 10 of them in sufficient quantities to start crystallization attempts. All 10 yielded crystals, and two structures have been solved. The structure of the sulfide-quinone oxidoreductase is the first available structure of this important family and allowed to draw valuable conclusions on the mechanism of action of this enzyme which is present from bacteria to man, and on its phylogenetic classification. The structure of the polar part of the respiratory complex I (NADH:ubiquinone oxidoreductase) could be determined at 2.9 Å. This enzyme is the first respiration chain complex involved into energy transduction and ROS reaction.