Thesis title: "Biophysical and Pharmacological Characterization of Cytoplasmic Dynein Heavy Chain 1"

Graduation date: 2010

MBSB PhD Advisor: Dr. Billy W. Day

Hikmat's research in the MBSB program involved characterizing the structure of cytoplasmic dynein heavy chain 1 (>380 kDa) using a combination of chemical labeling, hydrogen/deuterium exchange mass spectrometry, and computational biology. Cytoplasmic dynein is an important motor protein that translocates in a retrograde manner along microtubules to transport various cargoes throughout the cell. Several of these cargoes have been associated with diseases including cancer, neurodegenerative diseases, and HIV, making cytoplasmic dynein an important target to study. Part of my research also involves identifying compounds that interact with cytoplasmic dynein to be used as inhibitors or activators. I have also done work investigating the use of biosensor surfaces (dual polarization interferometry and resonant mirror) to assemble microtubules and further characterize their interactions with microtubule-perturbing agents. Microtubules are responsible for several important functions including maintaining cell structure, signaling, and cell division, particularly during mitosis, by physically separating chromosomes and orienting the plane of cleavage. These roles are a function of microtubule dynamics, the relative rates of assembly and disassembly at both the plus and minus ends of the microtubules. Increased microtubule dynamics is a hallmark of cancer cells, which makes microtubules a target for several anti-tumor therapeutics.

Current location: Scientist with molecular services company Hematogenix, in Chicago.

Current email:


B.S. in Physics, Allegheny College (Aug. 2002. - May. 2006)
Ph. D.  in Molecular Biophysics and Structural Biology Program, University of Pittsburgh, USA (2010)