Elka R. Georgieva

This study measures the binding affinity and conformational changes of Ca2+-calmodulin interacting with HIV-1 MA peptides, revealing structural and energetic features of the interaction.

This study quantifies HIV-1 Vpu's interaction with calmodulin using eFRET, showing that full-length Vpu has the highest binding affinity, while mutations and truncations reduce stability.

This study shows that soluble HIV-1 Vpu forms an equimolar complex with Ca2+-calmodulin, causing conformational changes and dissociation of Vpu oligomers.

The paper examines small viral proteins in cellular membranes, highlighting their structural diversity and the need for a multi-pronged approach to understand their function and conformational dynamics.