Dr. Jerry LaRue
Human immunodeficiency virus (HIV) attacks the immune system and if left untreated, could cause acquired immunodeficiency syndrome (AIDS). The HIV matrix protein (HIV-MA) is involved in replication and regulation of the HIV virus. Calmodulin (CaM), a calcium-binding protein found in all eukaryotes, has a potential role in the viral replication of HIV-MA which plays a key role in the replication of HIV. In order to investigate the interactions between calmodulin and the HIV-MA, a series of titrations with CaM are performed using circular dichroism. Circular dichroism (CD) uses circularly polarized light to observe the secondary structure of a molecule. The circularly polarized light is broken up into left and right components. When the molecule contains a chiral center, the left and right components are absorbed to different extents, and the differential absorption is measured with CD. Through a series of titrations, the chemical environment is changed in small increments so the molecule will experience conformational changes. As the conformation changes, CD is used to measure the ellipticity which provides a better understanding of the secondary structure that is a result of these chemical interactions. Since CaM plays a potential role in the viral replication of HIV-MA, CD is used to investigate the protein-protein interactions and conformational changes.
Sandoval, Andrea; Mau, D.; Karimi, N.; Sakamaki, K.; Owens, C.; and LaRue, Jerry, "Analyzing Interactions of Calmodulin with HIV-1 Matrix Protein" (2022). Student Scholar Symposium Abstracts and Posters. 561.