Department of Chemistry
Isaac, B., Gallagher, G. J., Balazs, Y. S., & Thompson, L. K., (2002) “Site-directed rotational resonance solid-state NMR distance measurements probe structure and mechanism in the transmembrane domain of the serine bacterial chemoreceptor“, Biochemistry 41, 3025-3036.
Murphy, O. J., III, Yi, X., Weis, R. M., & Thompson, L. K. (2001) “Hydrogen exchange reveals a stable and expandable core within the aspartame receptor cytoplasmic domain“, J. Biol. Chem. 276, 43262-43269.
Murphy, O. J., III, Kovacs, F. A., Sicard, E., & Thompson, L. K. (2001) “Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor“, Biochemistry 40, 1358-1366.
Balazs, Y. S. & Thompson, L. K. (1999) “Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance,” J. Mag. Res. 139, 371-376.
Kumashiro, K. K., Schmidt-Rohr, K., Murphy, O.J., III, Ouellette, K. L., Cramer, W. A., Thompson, L. K. (1998) “A Novel Tool for Probing Membrane Protein Structure: Solid-State NMR with Proton Spin Diffusion and X-Nucleus Detection,” J. Am. Chem. Soc. 120, 5043-5051.
Wang, J., Balazs, Y. S., & Thompson, L. K. (1997) “Solid-state REDOR NMR distance measurements at the ligand site of a bacterial chemotaxis membrane receptor,” Biochemistry 36, 1699-1703.
Parkhe, A. D., Seeley, S. K., Gardner, K., Thompson, L., & Lewis, R. V., (1997) “Structural Studies of Spider Silk Proteins in the Fiber“, J. Molecular Recognition 10, 1-6.
Seeley, S. K., Wittrock, G. K., Thompson, L. K., & Weis, R. M. (1996) “Oligomers of the Cytoplasmic Fragment from the Escherichia coli Aspartate Receptor Dissociate Through an Unfolded Transition State,” Biochemistry 35, 16336-16345.
Seeley, S. K., Weis, R. M., & Thompson, L. K. (1996) “The Cytoplasmic Fragment of the Aspartate Receptor Displays Globally Dynamic Behavior“, Biochemistry 35, 5199-5206.
Wang, J., Parkhe, A. D., Tirrell, D. A., & Thompson, L. K. (1996) “Crystalline Aggregates of the Repetitive Polypeptide {(AlaGly)3GluGly(GlyAla)3GluGly}10: Structure and Dynamics by 13C Magic Angle Spinning Nuclear Magnetic Resonance Spectroscopy“, Macromolecules 29, 1548-1553.