My research program involves synergistic studies of protein folding and design, protein-RNA interactions, phosphorylation, signaling, and function with both experimental and computational components. The research is based on the premise that rigorous and innovative studies of basic processes have broad implications in many areas of biological research. My lab employs a range of experimental and computational methods including hydrogen exchange (HX), NMR, small-angle X-ray scattering (SAXS), rapid mixing methods, mass spectrometry, molecular dynamics and home-grown coarse-grain folding simulations and modeling. I am a very a strong believer in collaboration, having co-mentored over twenty students and post-doctoral fellows who produce over 60 papers in the last 20 years. I have a history of developing multi-approaches to bear on a problem. Since my Ph.D. in low temperature physics in 1989, I have entered many different areas, including delineating protein and RNA folding pathways and denatured states, de novo structure prediction, and the design of light-sensitive allosteric proteins.
Harvard University
Cambridge
Ph.D. - Applied Physics
1989
University of California
San Diego
B.A. - Physics
1983
How hydrophobicity, side chains, and salt affect the dimensions of disordered proteins.
How hydrophobicity, side chains, and salt affect the dimensions of disordered proteins. Protein Sci. 2024 May; 33(5):e4986.
PMID: 38607226
An adaptive biomolecular condensation response is conserved across environmentally divergent species.
An adaptive biomolecular condensation response is conserved across environmentally divergent species. Nat Commun. 2024 Apr 11; 15(1):3127.
PMID: 38605014
HDX-MS finds that partial unfolding with sequential domain activation controls condensation of a cellular stress marker.
HDX-MS finds that partial unfolding with sequential domain activation controls condensation of a cellular stress marker. Proc Natl Acad Sci U S A. 2024 Mar 26; 121(13):e2321606121.
PMID: 38513106
Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.
Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility. Elife. 2023 Dec 06; 12.
PMID: 38054956
Folding of Prestin's Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility.
Folding of Prestin's Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility. bioRxiv. 2023 Oct 01.
PMID: 36909622
AlphaFold developers Demis Hassabis and John Jumper share the 2023 Albert Lasker Basic Medical Research Award.
AlphaFold developers Demis Hassabis and John Jumper share the 2023 Albert Lasker Basic Medical Research Award. J Clin Invest. 2023 Sep 21.
PMID: 37731359
An adaptive biomolecular condensation response is conserved across environmentally divergent species.
An adaptive biomolecular condensation response is conserved across environmentally divergent species. bioRxiv. 2023 Jul 29.
PMID: 37546789
Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.
Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation. Int J Mol Sci. 2023 Jan 31; 24(3).
PMID: 36768981
LILAC: enhanced actin imaging with an optogenetic Lifeact.
LILAC: enhanced actin imaging with an optogenetic Lifeact. Nat Methods. 2023 02; 20(2):214-217.
PMID: 36717692
Development of in vivo HDX-MS with applications to a TonB-dependent transporter and other proteins.
Development of in vivo HDX-MS with applications to a TonB-dependent transporter and other proteins. Protein Sci. 2022 09; 31(9):e4402.
PMID: 36040258