Congratulations to Jhullian Alston for being selected for the 2020 MilliporeSigma Fellowship
Jhullian Alston (JJ) is a fourth-year graduate student in the Biochemistry, Biophysics, and Structural Biology (BBSB) program. He is completing his Ph.D. thesis work jointly between the labs of Dr. Andrea Soranno and Dr. Alex Holehouse, where he combines computational biophysics with single-molecule fluorescence spectroscopy to understand how intrinsically disordered regions within a protein can affect interactions with both proteins and nucleic acids.
Jhullian joined the BBSB program after receiving his B.A. in Biology from The University of Maryland, Baltimore County where he was a Meyerhoff and MARC Scholar. Prior to starting his Ph.D. work, Jhullian had a diverse research background, studying nerve injury after radical prostatectomy, developing mouse models of prostate cancer, using CRISPR to develop fusion proteins in P. falciparum and C. elegans, and investigating the effects of O-GlcNAcylation.
Since joining the labs of Dr. Andrea Soranno and Dr. Alex Holehouse, both Assistant Professors in the Department of Biochemistry and Molecular Biophysics, Jhullian has studied how intrinsically disordered regions bind and condense nucleic acids, with an initial focus on how the telomeric protein TRF2, with its highly positively charged N-terminal intrinsically disordered region, mediates telomere compaction. While working on TRF2 he applied coarse grained simulations to model how specific binding motifs affect single chain condensation of polymers to better understand nucleic condensation. This led to him becoming intrigued by another example of nucleic acid condensation, the packaging of the SARS-CoV-2 viral genome. The SARS-CoV-2 Nucleocapsid protein, which contains three intrinsically disordered regions, is responsible for the packaging of the viral genome of SARS-CoV-2 virus. Yet how the Nucleocapsid protein drives selective genome packaging is still poorly understood. He has applied coarse grained and all-atom simulations to understand the selective condensation of RNA mediated by the nucleocapsid protein while providing a detailed conformational description of the protein. This current investigation has laid the groundwork for interrogating how conformational changes of the Nucleocapsid protein, upon binding to specific RNA sequences, modulates its ability to condense single and multiple RNA molecules. To answer this question, he will use atomistic and coarse-grained simulations, in concert with single molecule Foerster Resonance Energy Transfer and Fluorescence Correlation Spectroscopy.
Jhullian currently serves on the Biochemistry and Molecular Biophysics departmental Student Liaison Committee and is the Co-Chair for the Association of Black Biomedical Graduate Students.