Postdoctoral position, NMR of phase separation and aggregation in RNP granules

A postdoctoral position is available in the group of Nicolas Fawzi at Brown University.

We study the structure, dynamics, and molecular interactions in protein self-assembly, phase separation into ribonucleoprotein (RNP) granules, and aggregate formation in neurodegenerative disease. Using a combination of NMR spectroscopy approaches including direct observation of in vitro RNP granule mimics and dark-state exchange saturation transfer (DEST) NMR, atomistic simulation, and biophysical and imaging methods, we determine high-resolution structure and dynamics of these species and their interactions with other macromolecules and potential therapeutic agents. These projects are funded by the NIH (R01) and a three year grant from the Human Frontier Science Program (joint with Sapun Parekh, Max Planck Institute for Polymer Research).

Lab information:

The laboratory has significant access to Bruker 500, 600, and 850 MHz NMR spectrometers equipped with cryogenic probes as well as x-ray crystallography equipment in a newly updated structural biology core facility. A full complement of instruments for biophysical characterization of proteins, nucleic acids and their complexes (ITC, CD, DSC, fluorescence, TEM, AFM) is available at core facilities in the building and across the campus.

The laboratory forms part of a Brown University's vibrant and growing community of structural biology researchers using NMR and x-ray crystallography. Brown is located in Providence, Rhode Island, a cosmopolitan but affordable city less than one hour by train from downtown Boston.

Candidates with a background in NMR and structural biology, should send a CV and the names of at least two references to . Extensive experience in protein NMR and protein expression and purification are desired. Experience in mammalian cell culture and eukaryotic protein expression systems is beneficial but not required. A second postdoctoral position may be available in the coming year.

Brown University is an equal opportunity employer.

Highlights from recent work:

Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation.
Ryan et al. Molecular Cell. 2018

A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing.

Wang and Conicella et al. EMBO J. 2018


Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity.

Monahan and Ryan et al. EMBO J. 2018


ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.

Conicella et al. Structure. 2016


Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II.

Burke et al. Molecular Cell. 2015


Best regards,


Nicolas Lux Fawzi, PhD

Assistant Professor of Medical Science

Brown University

Department of Molecular Pharmacology, Physiology & Biotechnology

70 Ship Street, Box G-E

Providence, RI, 02912-G
(401) 863-5232