NMR studies on calcium-induced conformational transitions in calmodulin
Nuclear magnetic resonance (NMR) spectroscopy was used in order to investigate the relationships between structure, dynamics and calcium binding in the intracellular regulatory protein, calmodulin. Calmodulin consists of two similar domains, each binding two calcium ions with positive cooperativity. The studies described in this thesis focus on the isolated C-terminal domain, TR2C, and two mutants
