Electron Microscopy reconstruction of the yeast vacuolar ATPase. Ribbon models for individual protein subunits have been fit to the electron density.
From the lab of Stephan Wilkens, PhD.
Alaji Bah, PhD
- Assistant Professor of Biochemistry and Molecular Biology
Research Programs and Affiliations
- Biochemistry and Molecular Biology
- Biomedical Sciences Program
Elucidate the structure, dynamics and functions of intrinsically disordered proteins and protein regions (IDPs/IDRs) and their biological regulation by Post-translational modifications.
Elucidate the structure, dynamics and functions of intrinsically disordered proteins and protein regions (IDPs/IDRs) and their biological regulation by Post-translational modifications. I am particularly interested in characterizing such regulation at atomic resolution using Nuclear Magnetic Resonance (NMR) spectroscopy and other biophysical tools such as microcalorimetry and fluorescence spectroscopic techniques. A recent and exciting emerging field in the IDP world is the realization that this class of proteins, either alone or in concert with Nucleic acids, can drive phase separation of biomolecules, resulting in the formation of membraneless organelles with extremely high protein concentrations. Such organelles form both within the cytoplasm (e.g. RNA granules) and the nucleus (e.g. nucleolus) as well as in the extracellular matrix (elastin coacervation). The goal of my lab is not only to understand the PTM-mediated conformational transitions (e.g. folded vs. disorder transitions) and/or monomer: phase-separation transitions in specific examples, but to also develop tools/protocols to enable characterization of such properties in other biological systems.
SUNY Distinguished Professor Emeritus
- Richard Cross, PhD
- David Turner, PhD