Rate My Professor Paul Robustelli

Paul Robustelli is the James O. Freedman Assistant Professor of Chemistry and Computational Molecular Science at Dartmouth College, where he has served since January 2020. He holds additional appointments in the Neukom Academic Cluster of Computational Science and the Department of Biochemistry and Cell Biology. Robustelli earned a B.A. in Chemistry with a minor in Mathematics from Pomona College in 2006 and a Ph.D. in Chemistry from the University of Cambridge in 2011, working with Michele Vendruscolo on protein structure determination from NMR chemical shifts. Following his doctorate, he was an NSF Postdoctoral Research Fellow at Columbia University Medical Center from 2011 to 2013 under Arthur G. Palmer III, studying conformational dynamics in protein function using NMR and simulations. From 2013 to 2019, he worked as a Scientist at D.E. Shaw Research, developing physical models for simulating folded and disordered protein states and elucidating small molecule binding to intrinsically disordered proteins.

The Robustelli laboratory develops and applies atomistic molecular dynamics simulations to provide atomic-level descriptions of biomolecular functional motions, particularly for intrinsically disordered proteins involved in biological processes and diseases. Research focuses on conformational dynamics, molecular recognition mechanisms, small molecule binding to disordered sequences, phase separation, aggregation, and rational design of small molecule and biologic modulators. Computational approaches are integrated with NMR spectroscopy, with access to high-throughput NMR facilities. Selected publications include 'Developing a molecular dynamics force field for both folded and disordered protein states' (Proceedings of the National Academy of Sciences, 2018), 'Water dispersion interactions strongly influence simulated structural properties of disordered protein states' (Journal of Physical Chemistry B, 2015), 'Structure of an intermediate state in protein folding and aggregation' (Science, 2012), 'The mechanism of coupled folding-upon-binding of an intrinsically disordered protein' (Journal of the American Chemical Society, 2020), and 'Molecular basis of small-molecule binding to α-synuclein' (Journal of the American Chemical Society, 2022). Robustelli received the 2024 Cottrell Scholar Award, providing $120,000 for research on disordered protein self-assembly and therapeutics alongside educational initiatives in computational chemistry. His scholarship includes NSF Graduate Research and Postdoctoral Fellowships, Gates Cambridge Scholarship, and invitations to speak at international workshops on disordered proteins and computational biophysics. With over 4,000 citations, his contributions advance force field development, IDP simulations, and drug design in structural biology.