Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsion
Article first published online: 29 APR 2013
© 2013 The Authors Journal compilation © 2013 FEBS
Volume 280, Issue 11, pages 2675–2687, June 2013
How to Cite
Hellstrand, E., Kukora, S., Shuman, C. F., Steenbergen, S., Thulin, E., Kohli, A., Krouse, B., Linse, S. and Åkerfeldt, K. S. (2013), Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsion. FEBS Journal, 280: 2675–2687. doi: 10.1111/febs.12269
- Issue published online: 23 MAY 2013
- Article first published online: 29 APR 2013
- Accepted manuscript online: 29 MAR 2013 09:46AM EST
- Manuscript Accepted: 26 MAR 2013
- Manuscript Revised: 11 MAR 2013
- Manuscript Received: 5 DEC 2012
- Swedish Research Council
- Royal Physiographic Society
- Crafoord Foundation
- Howard Hughes Medical Institute to Haverford College
- Koshland Integrated Science Center Program at Haverford College
Fig. S1. Fluorescence emission spectra (500–660 nm) at 25 °C for CaM-D and CaM-DA (excitation at 480 nm) in 2 mm Tris/HCl pH 7.5 without and with 150 mm KCl.
Fig. S2. GuHCl denaturation of Ca4-CaM (CaM in Tris/HCl, pH 7.5, with 10 mm CaCl2) as monitored by the ellipticity at 222 nm.
Fig. S3. Binding of smMLCK-peptide to CaM-DA.
Fig. S4. SDS polyacrylamide gel electrophoresis.
Fig. S5. Peak deconvolution from absorbance spectra of FRET-CaM.
Table S1. Distance between the α-carbons of residues 17 and 117 in available NMR and X-ray structures of calmodulin.
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