Abstract
Abstract: Caldesmon (CaD) is associated with the thin filaments of smooth muscle tissues. Limited proteolysis studies of CaD reveal that the sequence w659 EKGNVF is involved in binding the calcium-regulatory protein calmodulin (CaM). Using transferred nuclear Overhauser enhancement NMR measurements, we have found that the 8 and 11 residue synthetic peptides KS(MWEKGNVF)S bind with an a-helical structure to CaM. Proton NMR titration studies show that a 2:1 peptide to CaM complex is formed, suggesting that the two domains of the dumbbell-shaped CaM can bind one equivalent of peptide each with similar binding constant.
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