Abstract
Calmodulin (CaM) is an important calcium (Ca2+) sensor in the cell and is able to activate over three hundred proteins to initiate cellular activities. CaM is a highly dynamic protein with a flexible central linker region joining the N‐terminal and C‐terminal domains. In each domain are two Ca2+ binding sites that cause structural changes to CaM when Ca2+ binds. These changes include the CaM central linker elongating and methionine rich hydrophobic patches being exposed, allowing for CaM to bind to the large population of target proteins. The structural interaction of CaM to short peptides from the CaM binding region of various target enzymes were investigated, including the nitric oxide synthase (NOS) enzyme.
Published Version
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