The exceptional versatility of calmodulin (CaM) three-dimensional arrangement is reflected
in the growing number of structural models of CaM/protein complexes currently available in …

Metal ions play crucial roles in numerous biological processes, facilitating biochemical
reactions by binding to various proteins. An increasing body of evidence suggests that …

Background—Genetic predisposition to life-threatening cardiac arrhythmias such as
congenital long-QT syndrome (LQTS) and catecholaminergic polymorphic ventricular …

This Handbook on Metalloproteins focuses on the available structural information of proteins
and their metal ion coordination spheres. It centers on the metal ions indispensable for life …

Cooperative calcium binding to the two homologous domains of calmodulin (CaM) induces
conformational changes that regulate its association with and activation of numerous cellular …

A microfluidic mixer is applied to study the kinetics of calmodulin conformational changes
upon Ca2+ binding. The device facilitates rapid, uniform mixing by decoupling …

We used nuclear magnetic resonance data to determine ensembles of conformations
representing the structure and dynamics of calmodulin (CaM) in the calcium-bound state (Ca …

Thioamides are single atom substitutions of the peptide bond that serve as versatile probes
of protein structure. Effective use of thioamides requires a robust understanding of the …

Chemical and thermal denaturation of calmodulin has been monitored spectroscopically to
determine the stability for the intact protein and its two isolated domains as a function of …

Here we report the structure of the widely utilized calmodulin (CaM)-dependent protein
kinase II (CaMKII) inhibitor KN93 bound to the Ca 2+-sensing protein CaM. KN93 is widely …