Dr Kathryn Scott

Systems Biology - Chemotaxis

I am a postdoctoral research associate working with Judy Armitage and Mark Sansom as part of the Oxford Centre for Integrative Systems Biology. My work involves applying computational and experimental methods to the study of Chemotaxis in Rhodobacter sphaeroides.

Beck, D.A.C., Jonsson, A.L., Schaeffer, R.D., Scott, K.A., Day, R., Toofanny, R.D., Alonso, D.O.V., and Daggett, V. (2008) Dynameomics: mass annotation of protein dynamics and unfolding in water by high-throughput atomistic molecular dynamics simulations. Protein Engineering Design and Selection. 21: 353-368.

Scott, K.A., Bond, P.J., Ivetec, A. Chetwynd, A.P., Khalid, S. and Sansom, M.S.P. (2008) Coarse-grained MD simulations of membrane protein-bilayer self-assembly. Structure. 16: 621-630.

Sansom, M.S.P., Scott, K.A., Bond, P.J. (2008) Coarse-grained simulation: a high-throughput computational approach to membrane proteins. Biochemical Society Transactions. 36: 27-32.

Scott, K.A., Alonso, D.O.V., Sato, S. Fersht, A.R. amd Daggett V. (2007) Conformational entropy of alanine versus glycine in protein dentatured states. PNAS 104: 2261-2666.

Scott, K.A., and Daggett V. (2007) Folding mechanisms of proteins with high sequence identity but different folds. Biochemistry. 46: 1545-1556.

Scott, K.A., Randles L.G., Moran, S.J., Daggett, V. and J. Clarke (2006) The Folding Pathway of Spectrin R17 from Experiment and Simulations: Using Experimentally Validated MD Simulations to Characterize States Hinted at by Experiment. Journal of Molecular Biology. 359: 159-173.

Scott, K.A., Alonso, D.O.V., Pan, Y. and V. Daggett. (2006) Importance of Context in Protein Folding: Secondary Structural Propensities versus Tertiary Contact-Assisted Secondary Structure Formation. Biochemistry. 45: 4153-4163.

Batey, S., Scott, K. A. & Clarke, J. (2006). Complex folding kinetics of a multidomain protein. Biophysical Journal. 90: 2120-2130.

Scott, K. A. & Clarke, J. (2005). Spectrin R16: Broad energy barrier or sequential transition states? Protein Science. 14: 1617-1629.

Scott, K. A., Batey, S., Hooton, K. A. & Clarke, J. (2004). The folding of spectrin domains I. Wild-type domains have the same stability but very different kinetic properties. Journal of Molecular Biology. 344: 195-205.

Scott, K. A., Randles, L. G. & Clarke, J. (2004). The folding of spectrin domains II. Phi-value analysis of R16. Journal of Molecular Biology. 344: 207-221.

Williams, P. M., Fowler, S. B., Best, R. B., Toca-Herrera, J. L., Scott, K. A., Steward, A. & Clarke, J. (2003). Hidden complexity in the mechanical properties of titin. Nature. 422: 446-449.

Scott, K. A., Steward, A., Fowler, S. B. & Clarke, J. (2002). Titin: a multidomain protein that behaves as the sum of its parts. Journal of Molecular Biology. 315: 819-829.