Dylan T Murray

The Murray lab focuses on understanding the physical chemistry of low sequence complexity protein domains and how these properties relate to their macroscopic behavior in cells. 30% of human proteins contain a domain that is biased towards a subset of the 20 natural amino acids and appear to be random semi-repetitive genetic gibberish. However, these domains are responsible for the formation of dynamic membraneless organelles during normal cellular function and mature into pathological aggregates in degenerative diseases such as amyotrophic lateral sclerosis (ALS). Chemically speaking, these structures correspond to biomolecular condensates, or protein phase separations, that exhibit varying degrees of dynamics and disorder. Although models have been developed to explain this behavior for simple chemical polymers, a comprehensive molecular-level understanding of how the more complex protein polymers transition into and between these phases remains elusive. We use nuclear magnetic resonance and other tools from physical chemistry to study the structure, thermodynamics, and kinetics of biomolecular condensates to achieve a more complete understanding of the fundamental physical chemistry underlying these fascinating cellular phenomena.

Education, Awards and Professional Highlights

• Appointed to UC Davis Faculty (2018)
• PRAT Postdoctoral Fellowship, National Institute of General Medical Sciences (2015-2018)
• Ph.D. Florida State University (2014)
• Michael Kasha Graduate Student Paper Award (2012)
• Florida State University Graduate Fellow (2008)
• Keynote Speaker, Sigma Xi Research Symposium, State University of New York at Plattsburgh (2007)
• B.S. State University of New York at Plattsburgh (2004)

Representative Publications

The most current list of publications can be found at Pubmed.

• Murray DT and Tycko R (2020) Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy. Biochemistry, 59(4):364-378.
• Murray DT, Zhou X, Kato M, Xiang S, Tycko R, McKnight SL (2018) Structural characterization of the D290V mutation site in hnRNPA2 low-compleixty-domain polymers. Proc. Nat. Acad. Sci., 115(42):9782-9791.
• Murray DT*, Kato M*, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R (2017) Structure of FUS Protein Fibrils and its Relevance to Self-assembly and Phase Separation of Low-Complexity Domains. Cell, 173(3):615-627. (Featured Cover Article – Artwork by DT Murray)
• Walti MA, Schmidt T, Murray DT, Wang H, Hinshaw JE, Clore GM (2017) Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein. Proc. Nat. Acad. Sci., 114(43): 9104-9109.
• Murray DT, Griffin J, Cross TA (2014) Detergent optimized membrane protein reconstitution in liposomes for solid state NMR. Biochemistry, 53(15): 2454-2463.
• Murray DT, Li C, Gao FP, Qin H, Cross TA (2014) Membrane protein structural validation by oriented sample solid-state NMR: diacylglycerol kinase. Biophys. J., 106(8): 1559-1569.
• Das N, Murray DT, Miao Y, Cross TA (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.
• Das N, Murray DT, Cross TA (2013) Lipid bilayer preparations of membrane proteins for oriented and magic angle spinning solid-state NMR samples. Nat. Prot., 8(11): 2256-2270.
• Cross TA, Murray DT, Watts A (2013) Helical membrane protein conformations and their environment. Eur. Biophys. J., 42(10): 731-755.
• Murray DT, Das N, Cross TA (2013) Solid state NMR strategy for characterizing native membrane protein structures. Acc. Chem. Res., 46(9): 2172-2181.
• Murray DT, Hung I, Cross TA (2013) Assignment of oriented sample NMR resonances from a three transmembrane helix protein. J. Magn. Reson., 240: 34-44.
• Murray DT, Lu Y, Cross TA, Quine JR (2011) Geometry of kinked protein helices from NMR data. J. Magn. Reson., 210: 82-89.

* Denotes authors contributed equally