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http://hdl.handle.net/1903/6787
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| Title: | A Biophysical Study of Clathrin Utilizing Light Scattering, Neutron Scattering and Structure Based Computer Modeling |
| Authors: | Ferguson, Matthew Lee |
| Advisors: | Nossal, Ralph J
Losert, Woflgang |
| Department/Program: | Physics |
| Type: | Dissertation |
| Sponsors: | Digital Repository at the University of Maryland
University of Maryland (College Park, Md.) |
| Keywords: | Physics, Molecular (0609)
Biophysics, General (0786)
Physics, Molecular (0609)
clathrin; light scattering; small angle neutron scattering; protein structure; protein flexibility; receptor mediated endocytosis |
| Issue Date: | 27-Apr-2007 |
| Abstract: | A principal component in the protein coats of certain post-golgi and endocytic
vesicles is clathrin, which appears as a three-legged heteropolymer (known as a triske-
lion) that assembles into polyhedral baskets principally made up of pentagonal and
hexagonal faces. In vitro, this assembly depends on the pH, with baskets forming
more readily at low pH and less readily at high pH. We have developed procedures,
based on static and dynamic light scattering, to determine the radius of gyration, Rg,
and hydrodynamic radius, RH, of isolated triskelia under conditions where basket
assembly occurs. Calculations based on rigid molecular bead models of a triskelion
show that the measured values can be accounted for by bending of the legs and a
puckering at the vertex. We also show that the values of Rg and RH measured for
clathrin triskelia in solution are qualitatively consistent with the conformation of
an individual triskelion that is part of a "D6 barrel" basket assembly measured ... |
| URI: | http://hdl.handle.net/1903/6787 |
| Appears in Collections: | Physics Theses and Dissertations
UM Theses and Dissertations
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Size | Format | No. of Downloads |
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| umi-umd-4273.pdf | | 2377Kb | Adobe PDF | 131 | View/Open |
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