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January 24, 2010 | History

Engineering of Halorhodospira halophila photoactive yellow protein 1 edition

Engineering of Halorhodospira halophila photoactive yellow protein
Stacy-Anne Morgan

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Engineering of Halorhodospira halophila photoactive yellow protein.

Published 2005 .
Written in English.

About the Book

Halorhodospira halophila photoactive yellow protein (PYP) is a promising candidate to act as a photoswitching domain in engineered proteins. Absorption of a photon of wavelength 446 nm triggers trans to cis isomerization of its 4-hydroxycinnamic acid chromophore leading to large structural perturbations in the protein's N-terminal region. In the dark, a slower cis to trans reisomerization of the chromophore occurs leading to restoration of the protein's native fold. Thus, fusion of proteins to PYP's N-terminus may enable modulation of the activity of the attached molecule by making use of the PYP photocycle.Site-directed mutagenesis was used to mutate the initiator ATG codon of PYP to TGC. This facilitates expression of PYP with an N-terminal cysteine allowing for N-terminal fusions to PYP using native chemical ligation. Our approach has been to use the amino thioacetic acid S-benzyl ester of 5-carboxy-tetramethylrhodamine (TMR),6, fluorophore, as well as S-Peptide for N-terminal attachment to PYP.

Edition Notes

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

Advisor: G. Andrew Woolley

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

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

GERSTEIN MICROTEXT copy on microfiche (1 microfiche).

The Physical Object

Pagination
70 leaves.
Number of pages
70

ID Numbers

Open Library
OL19216389M
ISBN 10
0494071494

History Created December 11, 2009 · 2 revisions Download catalog record: RDF / JSON

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