The interaction of melittin with calmodulin and its tryptic fragments |
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| Authors: | R F Steiner L Marshall D Needleman |
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| Affiliation: | 1. Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA;2. Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, Chapel Hill, NC 27599, USA;3. Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, 101 Manning Drive, Chapel Hill, NC 27514, USA;1. Albert-Ludwigs-Universität Freiburg, Institut für Biochemie, Albertstr. 21, 79104 Freiburg i. Br., Germany;2. Deutsches Elektronen-Synchrotron DESY, CFEL, Notkestr. 85, Hamburg, Germany;3. Delft University of Technology, Department of Biotechnology, Julianalaan 67, 2628 BC Delft, The Netherlands |
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| Abstract: | Melittin has been found to interact with both the N- and C-terminal half-molecules of calmodulin, as well as the intact molecule, in the presence of Ca2+. The interaction results in a major change in the microenvironment of Trp-19, which is in a more nonpolar, solvent-shielded, and immobilized microenvironment in the complex. The properties of Tyr-99 and Tyr-138 of calmodulin are altered by complex formation. From measurements of the efficiencies of radiationless energy transfer from Trp-19 to the nitro derivatives of Tyr-99 and/or Tyr-138, it is concluded that Trp-19 is located in proximity to the C-terminal lobe of calmodulin in the complex. |
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