Abstract
Ion channels are proteins in the lipid cell membrane. They spontaneously fluctuate between conformational shapes that are open or closed to the passage of ions. The ionic currents through an individual channel can be resolved by the patch clamp technique. Thus, the time sequence of open and closed conformational states can be measured in one channel molecule. The probability density function of the dwell times in the open and closed states displays scaling functions that may arise from: (1) a large number of conformational substates having a continuous distribution of activation energy barriers, (2) time-dependent changes in the energy barriers between states, or (3) local interactions that constrain local structures which interact hierarchically to form global structure.
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Liebovitch, L.S. Interpretation of protein structure and dynamics from the statistics of the open and closed times measured in a single ion-channel protein. J Stat Phys 70, 329–337 (1993). https://doi.org/10.1007/BF01053971
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DOI: https://doi.org/10.1007/BF01053971