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Fellows Directory

David Trentham

Dr David Trentham FRS


Elected: 1982


The mechanisms of chemical to mechanical energy transduction in muscle, and the regulation of this process in different types of muscle, have been the most important theme of David Trentham’s research — illustrated here by one example. Remarkably, the equilibrium constant of ATP hydrolysis when ATP is attached to myosin, a central protein of muscular contraction, is several orders of magnitude smaller than that in water. The hydrolysis was one of seven steps characterised during myosin ATPase activity. These steps incorporate well into the Lymn–Taylor biochemical model of contraction.

Further understanding of the biochemical mechanism occurred when related studies enabled the ATPase to be explored in muscle fibres capable of performing mechanical work. When combined with structural studies, we have a firm basis for understanding the molecular mechanism and for confirming the 1954 sliding filament hypothesis of muscular contraction. Technically, research problems have been addressed primarily around synthetic organic and especially nucleotide chemistry, transient kinetic methods — in particular, stopped-flow, oxygen-isotope exchange studies and photochemistry in which laser flash photolysis was used to initiate biological processes.

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