%0 Journal Article %1 Bray2013 %A Bray, Dennis %D 2013 %J Journal of Molecular Biology %K protein clusters %N 9 %P 1410 - 1414 %R 10.1016/j.jmb.2012.12.008 %T The Propagation of Allosteric States in Large Multiprotein Complexes %U http://www.sciencedirect.com/science/article/pii/S0022283612009412 %V 425 %X Abstract A statistical view of allostery leads to a more nuanced and physically realistic picture of protein cooperativity. If the conformational state of one protein molecule in a multiprotein complex influences the probability of a particular conformation in a neighbouring protein, then changes can propagate. Given suitable parameters, linear or two-dimensional arrays of allosteric subunits will then behave similar to an Ising model, exhibiting hypersharp responses to external conditions. Predictions based on this concept find good quantitative agreement in a number of experimental systems including switching of the bacterial flagellar motor, amplification of ligand signals in the Escherichia coli chemotaxis receptors, and termination of calcium sparks in cardiac muscle. A similar mechanism could potentially provide a universal mechanism of integration within living cells.

@article{Bray2013, abstract = {Abstract A statistical view of allostery leads to a more nuanced and physically realistic picture of protein cooperativity. If the conformational state of one protein molecule in a multiprotein complex influences the probability of a particular conformation in a neighbouring protein, then changes can propagate. Given suitable parameters, linear or two-dimensional arrays of allosteric subunits will then behave similar to an Ising model, exhibiting hypersharp responses to external conditions. Predictions based on this concept find good quantitative agreement in a number of experimental systems including switching of the bacterial flagellar motor, amplification of ligand signals in the Escherichia coli chemotaxis receptors, and termination of calcium sparks in cardiac muscle. A similar mechanism could potentially provide a universal mechanism of integration within living cells. }, added-at = {2013-05-31T16:04:00.000+0200}, author = {Bray, Dennis}, biburl = {https://www.bibsonomy.org/bibtex/2b3635221ffd7b90c1aac6994821fd1ff/quantentunnel}, doi = {10.1016/j.jmb.2012.12.008}, groups = {public}, interhash = {82523cb3f0a12f8a0e484766c6d593e1}, intrahash = {92ab82526b944eb3613c54739cf7d206}, issn = {0022-2836}, journal = {Journal of Molecular Biology}, keywords = {protein clusters}, number = 9, pages = {1410 - 1414}, timestamp = {2014-03-14T11:35:09.000+0100}, title = {The Propagation of Allosteric States in Large Multiprotein Complexes }, url = {http://www.sciencedirect.com/science/article/pii/S0022283612009412}, username = {quantentunnel}, volume = 425, year = 2013 }