Calmodulin (CaM) is a calcium sensing protein that plays a vital role in regulating within cell signaling pathways. CaM binds to its targets while also bound to calcium, which allows for it to have an altered conformation. When it is bound to four calcium ions it can cause disordered regions of its ligands to form a helical structure. This altered structure allows CaM to bind to many different targets. Disruptions of calcium signaling pathways CaM is involved in are also associated with several different neurological diseases, such as Alzheimer’s Disease. PEP-19 is a disordered protein that binds to CaM and alters its calcium binding kinetics and target protein binding. Along with understanding how CaM and PEP-19 behave when binding, it is vital to understand how the protein surfaces of CaM and PEP-19 behave in the biological setting. The behavior of the surface is normally observed <i>in vitro</i>, which might not represent how it behaves in a living organism. We plan to observe the physiological role played by the surface of CaM and PEP-19 by measuring the equilibrium thermodynamics and kinetics in living <i>E. coli</i>. This will be done by labeling CaM and PEP-19 with fluorine and then using NMR to observe the behavior of the folded and unfolded states of the proteins.

Investigation of calmodulin and PEP-19 surfaces in biological systems

ACS Spring 2022

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