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Biophys J, September 2001, p. 1333-1344, Vol. 81, No. 3
Division of Biology, California Institute of Technology, Pasadena, California 91125 USA
Interaction between a protein and a series of binding
sites on a cytoskeletal substrate can create a resistance, or
"protein friction," as the protein is moved along the substrate. If
attachment and detachment rates are specified asymmetrically, this
resistance can depend on the direction of movement, and the binding
interaction acts as a ratchet. Stochastic computer simulations have
been used to examine this type of protein-protein interaction. The
performance of a protein-protein ratchet in the piconewton and
nanometer range is significantly limited by thermal fluctuations, which
in experimental measurements with single molecules are evident as
Brownian motion. Simulations with a two-component model combining a
conventional motor enzyme model with a protein-protein ratchet confirm
previous suggestions that the processive movement of a single motor
enzyme molecule against a load, as seen in experiments with inner arm dynein molecules, might be made possible by an accessory protein interaction that prevents backward slippage. When this accessory protein interaction is defined so that it acts as a ratchet, backward slippage can be prevented with minimal interference with forward progression.
Biophys J, September 2001, p. 1333-1344, Vol. 81, No. 3
© 2001 by the Biophysical Society 0006-3495/01/09/1333/12 $2.00
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