Department of Chemistry
Malik, N. and Thompson, L. (2020) “Beyond Structure: Understanding dynamics in membrane protein complexes,” in: Separovic, F., Sani, M.-A. (Eds.), Solid-State NMR: Applications in Biomembrane Structure, Biophysical Society-IOP ebook, pp. 13–1 to 13–23.
Malik, N., Wahlbeck, K. A., and Thompson, L. K. (2020) “Strategies for identifying dynamic regions in protein complexes: flexibility changes accompany methylation in chemotaxis receptor signaling states” BBA Biomembranes 1862, 183312.
Kashefi, M., Malik, N., Struppe, J. O., and Thompson, L. K. (2019) “Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins” Journal of Magnetic Resonance 305, 5–15.
Kashefi, M. and Thompson, L.K. (2017) “Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR” J Physical Chemistry B 121, 8693-8705.
Harris, M.J., Struppe, J.O., Wylie, B.J., McDermott, A.E., and Thompson, L.K. (2016) “Multidimensional Solid-State NMR of a Functional Multiprotein Chemoreceptor Array” Biochemistry 55, 3616-3624.
Harris, M.J. and Thompson, L.K. (2014) “A Promising Prognosis for Solid State NMR of Functional Membrane Protein Complexes”, invited chapter for Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides, (F. Separovic and A. Naito, Eds.), RSC Publishing, 405-424.
Fowler, D.J., Harris, M.J., and Thompson, L.K. (2012) “Heat management strategies for solid-state NMR of functional proteins”, J. Mag. Res. 222, 112-118.
Thompson, L. K. (2011) “Solid State NMR of Membrane Proteins: Moving Towards Greater Complexity”, Annual Reports on NMR Spectroscopy 73, 127-158.
Fowler, D. J., Khalifah, P. G., and Thompson, L. K. (2010) “Design and characterization of a calixarene inclusion compound for calibration of long-range carbon–fluorine distance measurements by solid-state NMR,” J. Mag. Res. 207, 153-157.
Fowler, D. J., Weis, R. M., and Thompson, L. K. (2010) “Kinase-active Signaling Complexes of Bacterial Chemoreceptors Do Not Contain Proposed Receptor-Receptor Contacts Observed in Crystal Structures”, Biochemistry 49, 1425-1434.