Evidence from sedimentation analysis indicates that kinesin undergoes a change in conformation with different ionic strength. At high ionic strength, kinesin is in an unfolded, extended conformation, but assumes a compact, folded conformation at low ionic strength. The folding is thought to involve interaction between the head (motor domain) of kinesin heavy chain and a region in the tail. See related paper by Hackney, D.D., Levitt, J.D. and Suhan J. (1992) J. Biol. Chem. 267:8696-8701. Figure contributed by David D. Hackney

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Copyright 1996-2003. All rights reserved.

Created 7 July 1996 20:00 GMT
Modified 21 February 2000 21:25 GMT