Department of Chemistry
Affiliated Faculty, Lawrence Berkeley National Laboratory
Structure, function, and dynamics of macromolecular assemblies
The Murray Lab is interested in the physical properties of condensed phases of biological macromolecules that assemble into membraneless organelles and pathogenic aggregates in living cells and tissues. We use nuclear magnetic resonance, fluorescence, electron microscopy, calorimetry, and other tools of physical chemistry to examine the structural, thermodynamic, and kinetic properties of these assemblies. Our results are important for understanding biological processes in RNA metabolism and aggregation pathways in neurodegenerative diseases. In another avenue of research, we collaborate with the Joint BioEnergy Institute at the Berkeley Lab, where we use spectroscopy to examine bioengineered plants for use as novel biofuels.
Grad Group Affiliations
Specialties / Focus
- Biochemistry and Molecular Recognition
- Computational and Theoretical Biology
- Dynamics and Biophysical Engineering
- CHE107A - Physical Chemistry for the Life Sciences
- CHE216 - Magnetic Resonance Spectroscopy
Honors and Awards
- PRAT Postdoctoral Fellow, National Institutes of Health
- Graduate University Fellow, Florida State University
- American Chemical Society
- Biophysical Society
- B.S. Physics, State University of New York
- Ph.D. Florida State University
1. Murray, D.T., Zhou, X., Kato, M., Xiang, S., Tycko, R., and McKnight, S.L. (2018) Structural characterization of the D290V mutation site in hnRNPA2 low-complexity-domain polymers. PNAS. 115, E9782-E9791.
2. Murray, D.T., Kato, M., Lin, Y., Thurber, K.R., Hung, I., McKnight, S.L., and Tycko, R. (2017) Structure of FUS protein fibrils and its relevance to self-assembly and phase Separation of low-complexity domains. Cell. 171, 615-627. Cover Article.
3. Walti, M.A., Schmidt, T., Murray, D.T., Wang, H., Hinshaw, J.E., and Clore, G.M. (2017) Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein. PNAS. 114, 9104-9109.
4. Murray, D.T., Griffin, J., and Cross, T.A. (2014) Detergent optimized membrane protein reconstitution in liposomes for solid state NMR. Biochemistry. 53, 2454-2463.
5. Murray, D.T., Li, C., Gao, F.P., Qin, H., and Cross, T.A. (2014) Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase. Biophys. J. 106, 1559-1569.
6. Das, N., Murray, D.T., Miao, Y., and Cross, T.A. (2014) Helical Membrane Protein Strategy for Success. In Advances in Biological Solid-State NMR: Proteins and Membrane Active Peptides. Eds. F. Separovic and A. Naito, Royal Society of Chemistry, 320-352.
7. Murray, D.T., Hung, I., and Cross, T.A. (2013) Assignment of oriented sample NMR resonances from a three transmembrane helix protein. J. Magn. Reson. 240, 34-44.
8. Das, N., Murray, D.T., and Cross, T.A. (2013) Lipid bilayer preparations of membrane proteins for oriented and magic angle spinning solid-state NMR samples. Nat. Prot. 8, 2256-2270.
9. Cross, T.A., Murray, D.T., and Watts, A. (2013) Helical membrane protein conformations and their environment. Eur. Biophys. J. 42, 731-755.
10. Murray, D.T., Das, N., and Cross, T.A. (2013) Solid state NMR strategy for characterizing native membrane protein structures. Acc. Chem. Res. 46, 2172-2181.
11. Murray, D.T., Lu, Y., Cross, T.A., and Quine, J.R. (2011) Geometry of kinked protein helices from NMR data. J. Magn. Reson. 210, 82-89.