Calcium-dependent stoichiometries of the KCa2.2 (SK) intracellular domain/calmodulin complex in solution
Researchers at the Center for Learning and Memory at the University of Texas at Austin and Wyatt Technology used a combination of SEC-MALS, CG-MALS, analytical ultracentrifugation and other techniques to determine how Ca2+ regulates calmodulin (CaM) binding to its target on SK. In this study, researchers utilized a Calypso and DAWN detector to measure the complexes that form at zero and at saturating Ca2+. The results indicate that complexes with stoichiometries other than 2SKp/2CaM are important in channel gating.
Halling, D. B.; Kenrick, S. A.; Riggs, A. F.; Aldrich, R. W. Journal of General Physiology 2014, 143, 231-252. DOI: 10.1085/jgp.201311007