Correction|
January 25 2010
Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation
J Gen Physiol (2010) 135 (2): 169.
data&figures
Data & Figures
contents
Contents
supplements
Supplements
references
References
related&metrics
Related & Metrics
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.
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.
1 February 2010
