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Struts, springs and crumple zones: protein structures under force

  • Author(s): Dill, Jesse
  • Advisor(s): Marqusee, Susan
  • et al.
Abstract

In this dissertation, I describe studies on the folding and unfolding of several proteins using a combination of bulk solution spectroscopy and force denaturation experiments with optical tweezers. The three proteins, bacteriophage T4 lysozyme, E. coli ribonuclease H, and the D. melanogaster notch ankyrin domain, have distinct topologies that deLine their unfolding pathways by limiting or granting access to partially-­‐folded, high-­‐energy intermediates under force. Some of these states were previously unobserved; others were known, but these experiments allowed us to gain further information about their role in governing the proteins' response to force. Together, the results described here illustrate the power of single-­‐molecule force spectroscopy for isolating and characterizing kinetically important protein conformations that would otherwise be difficult or impossible to study.

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