Sahana Shah
Sahana is a rising junior studying the structure and function of intrinsically disordered proteins (IDPs) using biophysical methods under Dr. Elisar Barbar at Oregon State University. There, her research project has focused on studying RNA interactions with the SARS-CoV-2 N protein linker region.
As an Amgen Scholar at UCLA, Sahana is conducting research under Dr. Joe Loo in the Departments of Chemistry and Biochemistry. Her research for the summer leverages top-down mass spectrometry to study the protein cytochrome c and its interaction with ATP. Cytochrome c, or cytc, is a soluble heme protein that plays an important role in the electron transport chain of the mitochondria. Cytc has an ATP-binding site of high affinity and specificity, which is highly conserved across different species. Previous biochemical and molecular dynamics simulations demonstrated that ATP can effectively stabilize protein structure and inhibit aggregation. Preliminary work in the Loo Lab has shown that bovine cytc was stabilized by nonspecific ATP binding but also promoted the formation of a cytc dimer at a certain concentration threshold, a novel discovery. The lab hopes to better characterize the binding between cytc and ATP and investigate if cytc dimerization is relevant in nature.
Sahana would like to thank Dr. Joe Loo, her graduate student mentor Jessie Le, and the rest of the Loo Lab for all of their guidance and support. She would also like to thank the Amgen Scholars Program at UCLA for this invaluable opportunity to grow as a scientist.
Sahana is a rising junior studying the structure and function of intrinsically disordered proteins (IDPs) using biophysical methods under Dr. Elisar Barbar at Oregon State University. There, her research project has focused on studying RNA interactions with the SARS-CoV-2 N protein linker region.
As an Amgen Scholar at UCLA, Sahana is conducting research under Dr. Joe Loo in the Departments of Chemistry and Biochemistry. Her research for the summer leverages top-down mass spectrometry to study the protein cytochrome c and its interaction with ATP. Cytochrome c, or cytc, is a soluble heme protein that plays an important role in the electron transport chain of the mitochondria. Cytc has an ATP-binding site of high affinity and specificity, which is highly conserved across different species. Previous biochemical and molecular dynamics simulations demonstrated that ATP can effectively stabilize protein structure and inhibit aggregation. Preliminary work in the Loo Lab has shown that bovine cytc was stabilized by nonspecific ATP binding but also promoted the formation of a cytc dimer at a certain concentration threshold, a novel discovery. The lab hopes to better characterize the binding between cytc and ATP and investigate if cytc dimerization is relevant in nature.
Sahana would like to thank Dr. Joe Loo, her graduate student mentor Jessie Le, and the rest of the Loo Lab for all of their guidance and support. She would also like to thank the Amgen Scholars Program at UCLA for this invaluable opportunity to grow as a scientist.