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
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging.
Design and Use of AsLOV2-Based Optogenetic Tools for Actin Imaging. Methods Mol Biol. 2025; 2840:89-100.
PMID: 39724346
Collapse and Protein Folding: Should We Be Surprised That Biothermodynamics Works So Well?
Collapse and Protein Folding: Should We Be Surprised That Biothermodynamics Works So Well? Annu Rev Biophys. 2025 May; 54(1):17-34.
PMID: 39689264
Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.
Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB. Proc Natl Acad Sci U S A. 2024 Dec 17; 121(51):e2412327121.
PMID: 39671178
Correction to "Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding".
Correction to "Trifluoroethanol Promotes Helix Formation by Destabilizing Backbone Exposure: Desolvation Rather than Native Hydrogen Bonding Defines the Kinetic Pathway of Dimeric Coiled Coil Folding". Biochemistry. 2024 Sep 03; 63(17):2233.
PMID: 39141840
Temperature-Dependent Fold-Switching Mechanism of the Circadian Clock Protein KaiB.
Temperature-Dependent Fold-Switching Mechanism of the Circadian Clock Protein KaiB. bioRxiv. 2024 May 21.
PMID: 38826295
Transcriptome-wide mRNA condensation precedes stress granule formation and excludes stress-induced transcripts.
Transcriptome-wide mRNA condensation precedes stress granule formation and excludes stress-induced transcripts. bioRxiv. 2024 May 02.
PMID: 38659805
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