Dependence upon conditions of the properties of specifically located fluorescent probes on wheat germ calmodulin

Robert F. Steiner; Richard Waldron; D. Juminaga

doi:10.1117/12.58268

1 April 1992 Dependence upon conditions of the properties of specifically located fluorescent probes on wheat germ calmodulin

Robert F. Steiner, Richard Waldron, D. Juminaga

Author Affiliations +

Proceedings Volume 1640, Time-Resolved Laser Spectroscopy in Biochemistry III; (1992) https://doi.org/10.1117/12.58268
Event: OE/LASE '92, 1992, Los Angeles, CA, United States

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.

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Robert F. Steiner, Richard Waldron, and D. Juminaga "Dependence upon conditions of the properties of specifically located fluorescent probes on wheat germ calmodulin", Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); https://doi.org/10.1117/12.58268

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