COLL 371 |
| Alex Evilevitch, Laurence Lavelle, Eric Raspaud, William M. Gelbart, and Charles M Knobler. Department of Chemistry and Biochemistry, University of California Los Angeles, 607 Charles E. Young Drive East, Box 951569, Los Angeles, CA 90095-1569 |
| The genome in double-stranded (ds) DNA bacterial viruses (phage) is encased/protected by a protein shell, the capsid. When the hollow tail of a phage binds to a receptor on the outer surface of a bacterial cell, there is a conformational change that opens the capsid and allows the DNA to be injected into the cell. The diameter of a capsid is orders of magnitude smaller than the length of the fully extended DNA and is comparable to its persistence length. As a result, there is large force associated with the confinement of the very stiff, charged chain that drives the ejection once the capsid is open. We will describe osmotic suppression measurements on solutions of phage that allow this force to be determined. The relation between the force and the length of the genome and the presence of condensing agents will also be discussed. *Work supported by NSF Grants CHE00-7931 and CHE99-88651. |
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Surface and Colloid Chemistry Award Symposium Honoring Joseph Zasadzinski
8:10 AM-12:10 PM, Wednesday, March 31, 2004 Marriott -- Orange County 3, Oral
Division of Colloid and Surface Chemistry |