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| | Professor David R Trentham FRS :Randall Division of Cell & Molecular Biophysics :King's College London |
 | | Thus Figure 1 shows how orientations of a-helices in the N-terminal domain of the regulatory protein troponin C change with respect to the actin filament on activation of skeletal muscle from its relaxed state through an increase in Ca2+-ion concentration. |
 | | Walker, J.W., Somlyo, A.V., Goldman, Y.E., Somlyo, A.P., and Trentham, D.R. Kinetics of smooth and skeletal muscle activation by laser pulse photolysis of caged inositol 1,4,5-trisphosphate. |
 | | Corrie, J.E.T., Brandmeier, B.D., Ferguson, R.E., Trentham, D.R., Hopkins, S.C., van der Heide, U.A., Goldman, Y.E., Sabido-David, C., Dale, R.E., Criddle, S. and Irving, M. Dynamic measurement of protein conformation shows tilt and twist of the myosin light-chain domain in muscle contraction. |
| www.kcl.ac.uk /schools/biohealth/research/randall/dtrentham.html (563 words) |
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