Jacob is currently studying at University of Wyoming. He joined Professor Ruxandra Dima and her graduate student Dale Merz. Jacob was very succesful in his research and presented his work at the ACS meeting in New Orleans spring of 2018.
Jacob investigated allosteric mechanism of peptide release in the molecular chaperone Hsp70. In more details Hsp70 is a two-domain molecular chaperone involved in maintaining cellular homeostasis. Its function results from mech. changes caused by hydrolysis of ATP in the N-terminal nucleotide binding domain (NBD) that alter the client binding affinity of the C-terminal substrate binding domain (SBD). To study the dynamics of client binding, we linked the C-terminus of Hsp70 to a client peptide by means of an unstructured, chimeric linker. Utilizing coarse-grained simulations in concert with laser optical tweezer experimetns, we investigated the effects of force applied at various points of the linker on the unfolding of the SBD. Initial results indicate that stabilization varies across the SBD β-sandwich subdomain: the N-terminal β strands can detach before or after disruption of the rest of the subdomain.
Here is a link to a video of Jacob describing his experience at the end of the REU program
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