| dc.contributor.advisor |
Stuart Licht. |
en_US |
| dc.contributor.author |
Farbman, Mary E |
en_US |
| dc.contributor.other |
Massachusetts Institute of Technology. Dept. of Chemistry. |
en_US |
| dc.date.accessioned |
2009-06-30T17:08:46Z |
|
| dc.date.available |
2009-06-30T17:08:46Z |
|
| dc.date.copyright |
2008 |
en_US |
| dc.date.issued |
2008 |
en_US |
| dc.identifier.uri |
http://hdl.handle.net/1721.1/46048 |
|
| dc.description |
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2008. |
en_US |
| dc.description |
Vita. |
en_US |
| dc.description |
Includes bibliographical references. |
en_US |
| dc.description.abstract |
CIpA, a member of the Hspl00/Clp subset of the AAA+ superfamily, is an energy-dependent chaperone, disassembling and remodeling its protein substrates. CIpA also serves as the ATPase component of the ClpAP protease, where it is resonsible for binding specific substrates and unfolding and translocating them into its partner ClpP, the proteolytic component of the complex. We have used single molecule and traditional biochemical experiments to probe the mechanism of the unfolding and translocation steps of ClpA's enzymatic activity. We have identified two states of varying substrate affinities and shown that the conformational switch between these states is responsible for protein translocation. We have also investigated ClpA's autounfolding activity and have demonstrated that though CIpA can disaggregate some substrates in vivo, it does not act as an autodisaggregase. |
en_US |
| dc.description.provenance |
Made available in DSpace on 2009-06-30T17:08:46Z (GMT). No. of bitstreams: 2
370438992.pdf: 45904987 bytes, checksum: 2b782f4bcdfec8d8ba6ea1c968ed7dcb (MD5)
370438992-MIT.pdf: 45904797 bytes, checksum: d7af4af424b18cd3d139f27e4b526b84 (MD5)
Previous issue date: 2008 |
en |
| dc.description.statementofresponsibility |
by Mary E. Farbman. |
en_US |
| dc.format.extent |
144, [1] p. |
en_US |
| dc.language.iso |
eng |
en_US |
| dc.publisher |
Massachusetts Institute of Technology |
en_US |
| dc.rights |
M.I.T. theses are protected by
copyright. They may be viewed from this source for any purpose, but
reproduction or distribution in any format is prohibited without written
permission. See provided URL for inquiries about permission. |
en_US |
| dc.rights.uri |
http://dspace.mit.edu/handle/1721.1/7582 |
en_US |
| dc.subject |
Chemistry. |
en_US |
| dc.title |
Mechanistic studies of the ClpAP protease/ |
en_US |
| dc.type |
Thesis |
en_US |
| dc.description.degree |
Ph.D. |
en_US |
| dc.contributor.department |
Massachusetts Institute of Technology. Dept. of Chemistry. |
en_US |
| dc.identifier.oclc |
370438992 |
en_US |
