1 April 1992 Dependence upon conditions of the properties of specifically located fluorescent probes on wheat germ calmodulin
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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.
© (1992) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Robert F. Steiner, Robert F. Steiner, Richard Waldron, Richard Waldron, D. Juminaga, 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); doi: 10.1117/12.58268; https://doi.org/10.1117/12.58268
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