Monday, August 3, 2009, 2:00 pm — Large Conference Room, Building 703
Large biomolecular complexes often challenge the limits of traditional high-resolution structural biology techniques, requiring alternative methodologies for the study of structure and particularly of dynamics. In the research presented, synchrotron x-ray footprinting has been used to complement conventional structural techniques to study the 1.3MDa ClpAP Protease complex, a molecular machine responsible for the dissolution of protein aggregates and the degradation of unwanted proteins. The results provide structural support for a previously proposed mechanism of substrate translocation and implicate the ClpP N-terminus in both substrate gating and enzymatic activity. Investigations of this and other difficult systems have driven the need for focusing of the white beam and subsequent development of robust beamline components and diagnostic tools.
Hosted by: Juergen Thieme
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