of Neuroscience, Cell Biology, & Anatomy
5.212A Research Bldg 17Route
: 0620 | Tel:
772-1309 | Fax
: (409) 747-2187 | email@example.com
Our lab is interested in the mechanism by which proteins respond to mechanical forces. A large fraction of the proteins have structural and thus also mechanical functions. Examples include muscle proteins (e.g. titin), cytoskeletal proteins (e.g. spectrin)
and proteins of the extracellular matrix (e.g. fibronectin). However, not much is known how single proteins respond to mechanical forces. Do they behave as simple springs or do they display more complex features? Do they share common set of design
principles and mechanical fingerprints?
We are currently studying the mechanical properties of elastin (an abundant component of connective tissue), polycystin-1 (a cell membrane receptor found mainly in kidney tubules) and projectin and
twitchin (titin-like protein found in Drosophila and C. elegans). We hypothesize that these proteins function as a mechanical sensors that regulates several processes, including cell growth and tissue morphogenesis. We are testing this hypothesis by directly
measuring their mechanical properties using novel Atomic Force Microscopy (AFM) techniques that are capable of tracking forced-induced conformational changes in single molecules.