special biophysics/biochemistry seminar from Dongping

[Zhong, Dongping]

Dear All:
I am hosting a special biophysics/biochemistry talk in 1080 (Robert Smith seminar room) Physica Research Building (PRB) at 4pm on Wednesday. The speaker is Prof. Amnon Horovitz from Dept. of Structural Biology, Weizmann Institute of Science (https://www.weizmann.ac.il/Structural_Biology/Horovitz/). Prof. Horovitz is well known on studies of protein allostery in complex systems. He used a variety of biophysical tools: mass spectrometry, single-molecue, structural tools, etc… If you really like to meet him , please let me know (he will arrive here at noon on Wednesday and leave on Thursday). Thanks.

The talk title and abstract is s follows:

Allostery in chaperonins: how and why
Chaperonins consist of two back-to-back stacked heptameric rings with a cavity at each end where protein folding can take place.  They assist protein folding by undergoing large conformational changes that are controlled by ATP binding and hydrolysis. The concerted Monod–Wyman–Changeux and sequential Koshland–Némethy–Filmer models of cooperativity are often used to describe such allosteric switching.  In general, however, it has been impossible to distinguish between these different allosteric models using ensemble measurements of ligand binding in bulk protein solutions.  In this talk, two approaches that break this impasse will be described: one that is kinetic and a second that is based on native mass spectrometry.  Using these approaches, it was possible to show that the chaperonin GroEL from E. coli undergoes concerted intra-ring conformational changes whereas its eukaryotic homologue CCT/TRiC undergoes sequential intra-ring conformational changes.  The impact of these different allosteric mechanisms on the folding functions of GroEL and CCT/TRiC will be discussed.

Best regards,

Dongping Zhong
Robert Smith Professor of Physics
Professor of Chemistry and Biochemistry
The Ohio State University
Tel: 614-292-3044
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