Conformational Spread: The Propagation of Allosteric States in Large Multiprotein Complexes

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• Prof. Dennis Bray, Emeritus Professor, Department of Physiology, Development and Neuroscience, University of Cambridge
• Friday 26 February 2016, 14:00-15:00
• Pippard Lecture Theater.

If you have a question about this talk, please contact Dr. Hernandez-Ainsa.

The phenomenon of allostery is conventionally described for small symmetrical oligomeric proteins such as haemoglobin. However, our work on the bacterial chemotaxis pathway leads us to the view that conformational changes can also propagate through extended lattices of protein molecules. We have explored the statistical mechanics of idealized linear and two-dimensional arrays of allosteric proteins and shown that, as in the analogous Ising models, arrays of closely packed units can show large-scale integrated behavior. Applied to the chemotaxis system, conformational spread can explain the switching characteristics of the flagellar motor and the high amplification of signals at the chemotactic receptors. Our analysis applies to a variety of other systems such as muscle ryanodine receptors, actin filaments, and offers a more realistic view of the transitions of haemoglobin molecules. We suggest that conformational spread could provide the basis of a condensed state circuitry in a living cell, able to integrate biochemical and biophysical events over hundreds of protein molecules

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