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Kristofor NyquistClass of 2010Undergraduate Institution: Washington State University Major: Physics with Biophysics Option Origin: Silverdale, WA Lab: Andreas Martin Location: 556 Stanley Hall Email: knyquist@berkeley.edu
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Research |
ClpXP is a bacterial protease consisting of the ATP-dependent unfoldase ClpX and the barrel-shaped peptidase ClpP, which as a complex is responsible for the quality control and regulation of the proteome. Exact mechanistic details of how the hexameric unfoldase uses the energy of ATP hydrolysis to recognize, unfold, and translocate targeted protein substrates remains obscured by bulk experiments.
In collaboration with members of the Bustamante lab, I am interested in understanding how this machine operates using a recently developed optical tweezers substrate unfolding and translocation assay.
In collaboration with members of the Bustamante lab, I am interested in understanding how this machine operates using a recently developed optical tweezers substrate unfolding and translocation assay.
