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Proceedings Paper

Dependence upon conditions of the properties of specifically located fluorescent probes on wheat germ calmodulin
Author(s): Robert F. Steiner; Richard Waldron; D. Juminaga
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Paper Abstract

The single tyrosine, Tyr-139, of wheat germ calmodulin provides an intrinsic fluorescent probe to monitor Ca2+-binding domain 4, while the single cysteine, Cys-27, provides a site for the attachment of an extrinsic fluorescent label to monitor the N-terminal lobe. This has resulted in a means of comparing the response of the N- and C- terminal regions to pH, ionic strength, and Ca2+ level. Ca2+ ligation decreases the mobility sensed by Tyr-139 at neutral pH, while a shift in pH to 5.2 results in a further decrease.

Paper Details

Date Published: 1 April 1992
PDF: 10 pages
Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); doi: 10.1117/12.58268
Show Author Affiliations
Robert F. Steiner, Univ. of Maryland/Baltimore County (United States)
Richard Waldron, Univ. of Maryland/Baltimore County (United States)
D. Juminaga, Univ. of Maryland/Baltimore County (United States)


Published in SPIE Proceedings Vol. 1640:
Time-Resolved Laser Spectroscopy in Biochemistry III
Joseph R. Lakowicz, Editor(s)

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