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.

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.

We are interested in understanding how proteins function at the atomic level, using solution NMR as one of our primary tools of investigation. NMR provides high-resolution structural information and can be used to characterize the conformational dynamics that allow proteins to access different functional states. We are using this information, along with data provided by other biophysical tools to address questions in: Bacterial cell division Membrane protein structural biology

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