Skip to main content
The Journal of General Physiology logoLink to The Journal of General Physiology
. 2010 Feb;135(2):169. doi: 10.1085/jgp.200810143011310c

Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation

Felix Findeisen, Daniel L Minor Jr
PMCID: PMC2812501

Volume 133, No. 3, March 2, 2009. Pages 327–343.

Please note that in the original Fig. 2, “103” was missing from the y axes. The correct figure appears below.

Figure 2.

Figure 2.

Glycine substitution in IS6-AID linker disrupts helical structure. (A) Mean residue ellipticity at 222 nm for IS6-AID linker peptide, and AAA and GGG mutant peptides as a function of TFE concentration. Peptide sequence is shown. Black highlights the site of the GGG and AAA mutations. (B) IS6-AID linker peptide CD spectra at a peptide concentration of 50 μM in 50% TFE.


Articles from The Journal of General Physiology are provided here courtesy of The Rockefeller University Press

RESOURCES