Interaction of calmodulin with regulatory peptides

Robert F. Steiner; D. Juminaga; Sharon Albaugh

doi:10.1117/12.182719

17 August 1994 Interaction of calmodulin with regulatory peptides

Robert F. Steiner, D. Juminaga, Sharon Albaugh

Proceedings Volume 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV; (1994) https://doi.org/10.1117/12.182719
Event: OE/LASE '94, 1994, Los Angeles, CA, United States

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.

Citation Download Citation

Robert F. Steiner, D. Juminaga, and Sharon Albaugh "Interaction of calmodulin with regulatory peptides", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182719

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