This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Abnormalities in cellular protein folding play a crucial role in many pathological conditions such as Alzheimers, cancer, and ischemia. The chaperonin system Tric plays a pivotal role in cellular protein folding. We propose to study the mammalian chaperone system Tric and its archeal homologue MM-cpn using small angle x ray scattering (SAXS) and compare it with its bacterial counterpart, the GroEL system. In the first phase of our study, we will perform a series of static and time-resolved measurements on the chaperonin system. Static and time-resolved work on the eukaryotic system Tric and the archeal chaperonin will comprise the bulk of our effort. The large conformational changes we expect with this chaperone system are best observed with SAXS and will likely provide important insights into this chaperone complex.
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