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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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Using force spectroscopy mode of Atomic Force Microscopy (AFM) one can measure physiologically relevant pN forces between an AFM tip and a biomolecule with a mean displacement resolution of about 0.1 nm. The last 15 years have witnessed an explosion of interest in single molecule force spectroscopy fueled by: 1) new possibilities to advance in protein folding, 2) possibilities to elucidate molecular mechanisms of various cellular processes, and diseases, and 3) efforts to understand the nanomechanical properties of proteins, polysaccharides and DNAs in order to design biomimetic and/or mechanically functional materials.
In this talk, I will present several examples of our AFM force spectroscopy data. First, I will concentrate on elucidating early folding events in a simple model protein from changes of molecular compliance and dissipation factors. Using such measurements, we hope to provide basic understanding of early folding events. Next, I will show how mechanical force can influence the rate and mechanisms of an enzymatic cleavage of a single disulfide bond embedded in a protein. Time permitting, I will present the results of mechanical unfolding of on a recombinant protein comprising an NRR domain from mammalian Notch 1. Notch is a transmembrane cell signaling protein, and understanding its mechanical properties at the single molecule level is expected to help elucidating Notch’s role in processes relevant to embryonic development, tissue homeostasis, and some breast cancers.
