Dr. Goto's research laboratory focuses on understanding at a molecular level how proteins achieve their specific functions. One of the principle techniques used in this research program is solution NMR since it can provide structural and dynamic information about proteins at an atomic level. A number of different proteins are currently under investigation, including those important for cell signaling, viral infection and cell division. Many of these proteins interact with cell membranes, in some cases requiring the development of new approaches more suitable for the study of this challenging class of proteins.
Selected publications
- Ramos, D., Ducat, T., Cheng, J., Eng, N.F., Dillon, J.A., Goto, N.K.. Conformation of the cell division regulator MinE: Evidence for interactions between the topological specificity and anti-MinCD domains. Biochemistry. 45: 459-601, 2006
- Wu, Y., Shih, S.C.C., Goto, N.K.. Probing the structure of the Ff bacteriophage major coat protein transmembrane helix dimmer by solution NMR. Biochim. Biophys. Acta 1768: 3206-3215, 2007
- Shih, S.C.C., Stoica, I., Goto, N.K.. Investigation of the utility of selective methyl protonation for determination of membrane protein structures. J. Biomol. NMR 42: 49-58, 2008
- Sherrat, A.R., Braganza, M.V., Nguyen, E., Ducat, T., Goto, N.K.. Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain. Biochim. Biophys. Acta, in press, 2009