| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5371554 | Biophysical Chemistry | 2011 | 10 Pages |
Abstract
âºRotation of the kinesin-14 Ncd stalk represents the motor power stroke. âºStructural data imply that stalk movement is required for motor-microtubule binding. âºWe show that the stalk rotates close to the microtubule upon motor binding to ATP. âºNcd stalk movement or rotation is thus proposed to occur in two steps. âºThis would produce a working stroke and step larger than the kinesin-1 8-nm step.
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Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Mark A. Hallen, Zhang-Yi Liang, Sharyn A. Endow,