臺大化學系 今日(9/20)學術演講訊息- Prof. Lee-Wei Yang (楊立威教授)
截止日期：2012-09-20
日期：2012/09/20（Thu.）
時間：自15時30分至17時00分
演講地點(地址): 原分所浦大邦講堂(Dr. Poe Lecture Hall, IAMS)
演講者: Prof. Lee-Wei Yang (楊立威 教授)
演講者職稱：Professor
演講者服務單位：Institute of Bioinformatics and Structural Biology, National Tsing Hua University
演講題目：Catalytic Chemistry Coupled with Mechanically Important Residues
【Abstract】
Recent studies point to the intrinsic ability of proteins to undergo necessary domain movements to facilitate biological functions. Such abilities appear to be conferred to a large extent by the contact topology, or the overall shape of a protein.
Toward establishing to what extent protein geometry dictates the collective motion of intact subunits in proteins, we performed an extensive analysis of the extent of enzyme catalytic sites involved in collective motions of proteins, and assessed if/how the molecular shape by itself determines the location of protein functional sites regardless of local chemistry on the primary sequence. The predicted important mechanical residues are found conserved in the evolution.
Our chemistry-free analysis demonstrates that active sites can be inferred to a good level of accuracy from knowledge of the overall shape of the enzyme, using fuzzy pictures with resolution as low as 30Å.
時間：自15時30分至17時00分
演講地點(地址): 原分所浦大邦講堂(Dr. Poe Lecture Hall, IAMS)
演講者: Prof. Lee-Wei Yang (楊立威 教授)
演講者職稱：Professor
演講者服務單位：Institute of Bioinformatics and Structural Biology, National Tsing Hua University
演講題目：Catalytic Chemistry Coupled with Mechanically Important Residues
【Abstract】
Recent studies point to the intrinsic ability of proteins to undergo necessary domain movements to facilitate biological functions. Such abilities appear to be conferred to a large extent by the contact topology, or the overall shape of a protein.
Toward establishing to what extent protein geometry dictates the collective motion of intact subunits in proteins, we performed an extensive analysis of the extent of enzyme catalytic sites involved in collective motions of proteins, and assessed if/how the molecular shape by itself determines the location of protein functional sites regardless of local chemistry on the primary sequence. The predicted important mechanical residues are found conserved in the evolution.
Our chemistry-free analysis demonstrates that active sites can be inferred to a good level of accuracy from knowledge of the overall shape of the enzyme, using fuzzy pictures with resolution as low as 30Å.