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January 24, 2010 | History

An intrinsic exciton probe reports methylene-unit resolution in the PagP hydrocarbon ruler 1 edition

An intrinsic exciton probe reports methylene-unit resolution in the Pa ...
Mohammad Adil Khan

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An intrinsic exciton probe reports methylene-unit resolution in the PagP hydrocarbon ruler.

Published 2005 .
Written in English.

About the Book

PagP, an outer membrane enzyme of Gram-negative bacteria, transfers a palmitate chain from phospholipids to lipid A to provide bacterial resistance against host immune defences. PagP acyl chain selection is determined by the hydrocarbon ruler. We have methylated the free sulfhydryl group at the floor of the hydrocarbon ruler in PagPG88C by using site-directed chemical labelling. The reaction was shown to be quantitative by using electrospray ionization mass spectrometry and resulted in the expected shift in PagP acyl-chain selection by a single methylene-unit. The detergent-refolded proteins were structurally characterized by circular dichroism spectroscopy, revealing an exciton couplet that was extinguished in the PagPG88C mutant and subsequently restored upon chemical methylation. We demonstrate that a local structural perturbation arising from the PagPG88C sulfhydryl group was associated with the loss of the exciton and a widening of the acyl-chain resolution. Consequently, the exciton reports methylene-unit resolution in the PagP hydrocarbon ruler.

Edition Notes

Source: Masters Abstracts International, Volume: 44-02, page: 0906.

Thesis (M.Sc.)--University of Toronto, 2005.

Electronic version licensed for access by U. of T. users.

GERSTEIN MICROTEXT copy on microfiche (2 microfiches).

The Physical Object

Pagination
125 leaves.
Number of pages
125

ID Numbers

Open Library
OL19217206M
ISBN 10
0494073721

History

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January 24, 2010 Edited by WorkBot add more information to works
December 11, 2009 Created by WorkBot add works page