Texas Tech University

Dr. Adam W. Smith

Dr. Smith

Title: Associate Professor

Education: Ph.D., Massachusetts Institute of Technology, 2008
Postdoctoral Associate, University of California, Berkeley, 2008 - 2011

Research Area: Biochemistry

Office:  Chemistry 413D

Phone: 806-834-3551

Email: AW.Smith@ttu.edu

Webpage: Research Group


Adam W. Smith was born in Texas and grew up in Utah. He was an undergraduate at the University of Utah and then earned a PhD at MIT in the lab of Andrei Tokmakoff studying peptide and protein folding with 2D IR spectroscopy. From 2008-2011 he was a postdoctoral researcher with Jay T. Groves at UC Berkeley, where he studied membrane protein structure and function with advanced fluorescence imaging and spectroscopy. In 2012, Adam was a visiting scientist at the National University of Singapore and Lawrence Berkeley National Laboratory. He joined the faculty at the University of Akron from 2012-2022 and then moved to Texas Tech University where he is currently an Associate Professor of Chemistry.

Principal Research Interests

Dr Smith's research interests are on the chemical interactions that regulate cell signaling in the plasma membrane. Membrane proteins are the primary target of pharmaceutical compounds, but their chemical environment is poorly understood. This is mainly due to the diversity of lipid and protein species in the plasma membrane and their complex organization. Determining how these chemical interactions control membrane protein function and ultimately cell behavior is still at an early stage, with many important discoveries yet to be made. The approach in the Smith Lab is to measure lipid-protein and protein-protein interactions with time-resolved fluorescence microscopy. Membrane protein oligomerization is probed in live cells and lipid-protein interactions are studied in model membranes. This work is inherently interdisciplinary; a physical/analytical chemistry perspective and methodology is combined with biochemistry and molecular biology to investigate the chemical details of cell signaling.


  • Brown, B.P., Y. Zhang, S. Kim, P. Finneran, Y. Yan, Z. Du, J. Kim, A.L. Hartzler, M.L. LeNoue-Newton, A.W. Smith, J. Meiler, and C.M. Lovly, (2022) Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer. PNAS, 2022. 119(30).
  • Du, Z.; Brown, B. P.; Kim, S.; Ferguson, D.; Pavlick, D. C.; Jayakumaran, G.; Benayed, R.; Gallant, J. N.; Zhang, Y.K.; Yan, Y.; Red-Brewer, M.; Ali, S. M.; Schrock, A. B.; Zehir, A.; Ladanyi, M.; Smith, A. W.; Meiler, J.; Lovely, C. M. (2021) Structure-function analysis of oncogenic EGFR Kinase Domain Duplication reveals insights into activation and a potential approach for therapeutic targeting. Nature Comm. 12, 1382.
  • Asher, W. B.; Geggier, P.; Holsey, M. D.; Gilmore, G. T.; Pati, A.; Meszaros, J.; Terry, D. S.; Mathiasen, S.; Kaliszewski, M. J.; McCauley, M. D.; Govindaraju, A.; Zhou, Z.; Harikumar, K. G. Jaqaman, K.; Miller, L. J.; Smith, A. W.; Blanchard, S. C.; Javitch, J. A. (2021) Single-Molecule FRET Imaging of GPCR Dimers in Living Cells. Nature Methods 18, 397-405.
  • Christie, S.; Shi, X.; Smith, A. W. (2020) Resolving Membrane Protein–Protein Interactions in Live Cells with Pulsed Interleaved Excitation Fluorescence Cross-Correlation Spectroscopy. Acc. Chem. Res. 53, 792-799.
  • Bogucki, R., M. Greggila, P. Mallory, J. Feng, K. Siman, B. Khakipoor, H. King and Smith, A. W. (2019). "A 3D-Printable Dual Beam Spectrophotometer with Multiplatform Smartphone Adaptor." Journal of Chemical Education, 96, 1527-1531.
  • Mallory, P., Gutierrez, E., Pinkevitch, M., Klinginsmith, C., Comar, W. D., Roushar, F. J., Schlebach, J. P., Smith, A. W. and Jastrzebska, B. (2018) The Retinitis Pigmentosa-Linked Mutations in Transmembrane Helix 5 of Rhodopsin Disrupt Cellular Trafficking Regardless of Oligomerization State. Biochemistry 57, 5188-5201.
  • Kaliszewski, M. J., Shi, X., Hou, Y., Lingerak, R., Kim, S., Mallory, P., Smith, A. W. (2018) Quantifying Membrane Protein Oligomerization with Fluorescence Cross-Correlation Spectroscopy. Methods 140-141, 40-51.
  • Zeng, Z., Shi, X., Mabe, T., Christie, S., Gilmore, G., Smith, A. W., and Wei, J. (2017) Protein Trapping in Plasmonic Nanoslit and Nanoledge Cavities: The Behavior and Sensing. Analytical Chemistry 89, 5221-5229.
  • Shi, X., Hapiak, V., Zheng, J., Muller-Greven, J., Bowman, D., Lingerak, R., Buck, M., Wang, B.-C., and Smith, A. W. (2017) A role of the SAM domain in EphA2 receptor activation. Scientific Reports 7, 45084.
  • Jastrzebska, B., Comar, W. D., Kaliszewski, M. J., Skinner, K. C., Torcasio, M. H., Esway, A. S., Jin, H., Palczewski, K., and Smith, A. W. (2017) A G Protein-Coupled Receptor Dimerization Interface in Human Cone Opsins. Biochemistry 56, 61-72.
  • Huang, Y., Bharill, S., Karandur, D., Peterson, S. M., Marita, M., Shi, X., Kaliszewski, M. J., Smith, A. W.*, Isacoff, E. Y.*, Kuriyan, J.*, (2016) Molecular Basis for Multimerization in the Activation of the Epidermal Growth Factor Receptor. eLife 5, e14107. *Joint corresponding authors
  • Smith, A. W., Huang, H. H., Endres, N. F., Rhodes, C., Groves, J. T. (2016) Dynamic Organization of Myristoylated Src in the Live Cell Plasma Membrane. Journal of Physical Chemistry B 120, 867-876.
  • Shi, X., Kohram, M., Zhuang, X., Smith, A. W. (2016) Interactions and translational dynamics of phosphatidylinositol bisphosphate (PIP2) lipids in asymmetric lipid bilayers. Langmuir 32, 1732-1741.
  • Liu, C., Wang, K., Yi, C., Shi, X., Smith, A. W., Gong, X., Heeger, A. J. (2016) Efficient Perovskite Hybrid Photovoltaics Via Alcohol-Vapor Annealing Treatment. Advanced Functional Materials 25, 101-110.
  • Grasse, E. K., Torcasio, M. H., Smith, A. W. (2016) Teaching UV–Vis Spectroscopy with a 3D-Printable Smartphone Spectrophotometer. Journal of Chemical Education 93, 146-151.
  • Marita, M., Wang, Y, Comar, W. D., Shi, X., Dasari, P., Zhang, X., and Smith, A. W. (2015) Class A plexins are organized as preformed inactive dimers on the cell surface. Biophysical Journal 109, 1937-1945.
  • Biswas, K. H., Hartman, K. L., Yu, C.-h., Harrison, O. J., Song, H., Smith, A. W., Huang, W. Y. C., Lin, W.-C., Guo, Z., Padmanabhan, A., Troyanovsky, S. M., Dustin, M. L., Shapiro, L., Honig, B., Zaidel-Bar, R., Groves, J. T., (2015) E-cadherin junction formation involves an active kinetic nucleation process. Proceedings of the National Academy of Sciences USA 112, 10932-10937
  • Liu, C., Wang, K., Yi, C., Shi, X., Du, P., Smith, A. W., Karim, A., Gong, X. (2015) Ultrasensitive Solution-Processed Perovskite Hybrid Photodetectors. Journal of Materials Chemistry C 3, 6600-6606.
  • Smith, A. W. (2015) Detection of Rhodopsin Dimerization In Situ by PIE-FCCS, a Time-Resolved Fluorescence Spectroscopy. Methods in Molecular Biology, RhodopsinB. Jastrzebska, editor. 1271, 205-219.
  • Shi, X., Li, X., Kaliszewski, M. J., Zhuang, X., and Smith, A. W. (2015) Tuning the Mobility Coupling of Quaternized Polyvinylpyridine and Anionic Phospholipids in Supported Lipid Bilayers. Langmuir 31, 1784-1791.
  • Comar, W. D., Schubert, S. M., Jastrzebska, B., Palczewski, K. and Smith, A. W. (2014) Mobility and clustering of the opsin G protein-coupled receptor in live cells with time-resolved fluorescence spectroscopy. Journal of the American Chemical Society 136, 8342.
  • Smoligovets, A. A., Smith, A. W., and Groves, J. T. (2013) Ratiometric Imaging of the T-Cell Actin Cytoskeleton Reveals the Nature of Receptor-Induced Cytoskeletal Enrichment. Biophysical Journal 105, L11-L13.
  • Endres, N. F.*, Das, R.*, Smith, A. W.*, Arkhipov, A., Kovacs, E., Huang, Y., Pelton, J.G., Shan, Y., Shaw, D.E., Wemmer, D.E., Groves, J.T., Kuriyan, J. (2013) Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor, Cell 152, 543-546. *Equal Contribution
  • Triffo, S. B., Huang, H. H., Smith, A. W., Chou, E. T., Groves, J. T. (2012) Monitoring Lipid Anchor Organization in Cell Membranes by PIE-FCCS. Journal of the American Chemical Society 134, 10833–10842.
  • Belardi, B., O'Donoghue, G. P., Smith, A. W., Groves, J. T., Bertozzi, C. R. (2012) Investigating Cell Surface Galectin-Mediated Cross-Linking on Glycoengineered Cells. Journal of the American Chemical Society 134, 9549.
  • Smith, A. W. (2012). Invited Review: Lipid-protein interactions in biological membranes: a dynamic perspective. Biochimica et Biophysica Acta – Biomembranes 1818, 172.
  • Smoligovets, A. A., Smith, A. W., Wu, H. J., and Groves, J. T. (2012) Characterization of dynamic actin associations with T-cell receptor microclusters in primary T cells. Journal of Cell Science 125, 725.
  • Smith, A. W., Smoligovets, A. A., and Groves, J. T. (2011) Patterned two-photon photoactivation illuminates spatial reorganization in live cells. Journal of Physical Chemistry A, 115, 3867-3875.
  • Smith, A. W., Lessing, J., Ganim, Z., Peng, C. S., Roy, S., Jansen, T. L. C., Knoester, J., and Tokmakoff, A. (2010) Feature Article: Melting of a β-hairpin peptide using isotope-edited 2D IR spectroscopy and simulations. Journal of Physical Chemistry B. 114, 10913.
  • Ganim, Z. Chung. H. S., Smith, A. W., DeFlores, L. P., Jones, K. C. and Tokmakoff, A. (2008) Amide I two-dimensional infrared spectroscopy of proteins. Accounts of Chemical Research 41, 432-441
  • Smith, A. W., and Tokmakoff, A. (2007) Probing local structural events in β-hairpin unfolding with transient nonlinear infrared spectroscopy. Angewandte Chemie International Edition 46, 7984-7987.
  • Chung, H. S., Khalil, M., Smith, A. W. and Tokmakoff, A. (2007) Transient 2D IR spectrometer for probing nanosecond temperature-jump kinetics. Review of Scientific Instruments 78, 063101
  • Smith, A. W., and Tokmakoff, A. (2007) Amide I two-dimensional infrared spectroscopy of β-hairpin peptides. Journal of Chemical Physics 126, 045109.
  • Smith, A. W., Chung, H. S., Ganim, Z., and Tokmakoff, A. (2006) Multidimensional IR Spectroscopy of Site-Specific Hairpin Folding. Proceedings of the 15th International Conference on Ultrafast Phenomena, Pacific Grove, CA.
  • Smith, A. W., Chung, H. S., Ganim, Z., and Tokmakoff, A. (2005) Residual native structure in a thermally denatured beta-hairpin. Journal of Physical Chemistry B 109, 17025-17027.
  • Chung, H. S., Khalil, M., Smith, A. W., Ganim, Z., and Tokmakoff, A. (2005) Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin. Proceedings of the National Academy of Sciences USA 102, 612-617.
  • Sickafoose, S. M., Smith, A. W., and Morse, M. D. (2002) Optical spectroscopy of tungsten carbide (WC). Journal of Chemical Physics 116, 993-1002.

Department of Chemistry & Biochemistry

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    1204 Boston Avenue, Lubbock, TX 79409-1061
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