Cargando…
Controlling Kinesin by Reversible Disulfide Cross-Linking: Identifying the Motility-Producing Conformational Change
Conventional kinesin, a dimeric molecular motor, uses ATP-dependent conformational changes to move unidirectionally along a row of tubulin subunits on a microtubule. Two models have been advanced for the major structural change underlying kinesin motility: the first involves an unzippering/zippering...
| Autores principales: | , |
|---|---|
| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
2000
|
| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174365/ https://www.ncbi.nlm.nih.gov/pubmed/11086009 |