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Proceedings Paper

Interaction of calmodulin with regulatory peptides
Author(s): Robert F. Steiner; D. Juminaga; Sharon Albaugh
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Paper Abstract

Dynamic fluorescence measurements of radiationless energy transfer between tryptophan donor groups located within the regulatory peptides Phk13 and Phk5 of glycogen phosphorylase kinase and nitrotyrosine acceptor groups within calmodulin or Phk13 have provided a set of separations and separation distributions which place definite restrictions upon the geometry of the peptide-calmodulin complexes. Phk13 appears to be bent into a hairpin-shaped (beta) -structure. The distributions of separations are suggestive of substantial internal mobility of the complex species.

Paper Details

Date Published: 17 August 1994
PDF: 11 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182719
Show Author Affiliations
Robert F. Steiner, Univ. of Maryland/Baltimore County (United States)
D. Juminaga, Univ. of Maryland/Baltimore County (United States)
Sharon Albaugh, Univ. of Maryland/Baltimore County (United States)


Published in SPIE Proceedings Vol. 2137:
Time-Resolved Laser Spectroscopy in Biochemistry IV
Joseph R. Lakowicz, Editor(s)

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