Dynamic hysteresis in a one-dimensional Ising model: application to allosteric proteins.
We solve exactly the problem of dynamic hysteresis for a finite one-dimensional Ising model at low temperature. We find that the area of the hysteresis loop, as the field is varied periodically, scales as the square root of the field frequency for a large range of frequencies. Below a critical frequency there is a correction to the scaling law, resulting in a linear relationship between hysteresis area and frequency. The one-dimensional Ising model provides a simplified description of switchlike behavior in allosteric proteins, such as hemoglobin. Thus our analysis predicts the switching dynamics of allosteric proteins when they are exposed to a ligand concentration which changes with time. Many allosteric proteins bind a regulator that is maintained at a nonequilibrium concentration by active signal transduction processes. In the light of our analysis, we discuss to what extent allosteric proteins can respond to changes in regulator concentration caused by an upstream signaling event, while remaining insensitive to the intrinsic nonequilibrium fluctuations in regulator level which occur in the absence of a signal.
Graham
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Biophysics Group, Cavendish Laboratory, Madingley Road, Cambridge CB3 0HE, United Kingdom. ig224@cam.ac.uk
Duke
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D000494:Allosteric Regulation; D000495:Allosteric Site; D001665:Binding Sites; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry*; D017711:Nonlinear Dynamics; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D013237:Stereoisomerism
D020409:Molecular Motor Proteins; D011506:Proteins