Kinesin as an Electrostatic Machine
Kinesin and related motor proteins utilize ATP fuel to propel themselves along the external surface of microtubules in a processive and directional fashion. We show that the observed step-like motion is possible through time-varying charge distributions furnished by the ATP hydrolysis cycle while th...
| Autores: | , , |
|---|---|
| Tipo de documento: | artigo |
| Data de publicação: | 2007 |
| País: | España |
| Recursos: | Universitat Politècnica de Catalunya (UPC) |
| Repositório: | UPCommons. Portal del coneixement obert de la UPC |
| Idioma: | inglês |
| OAI Identifier: | oai:upcommons.upc.edu:2117/425712 |
| Acesso em linha: | https://hdl.handle.net/2117/425712 https://dx.doi.org/10.1007/s10867-006-9028-6 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Kinesin electrostatics Tubulin dipole moment Neck domain ATP hydrolysis Microtubule directionality Kinesin processivity Kinesin substep Àrees temàtiques de la UPC::Física |
| Resumo: | Kinesin and related motor proteins utilize ATP fuel to propel themselves along the external surface of microtubules in a processive and directional fashion. We show that the observed step-like motion is possible through time-varying charge distributions furnished by the ATP hydrolysis cycle while the static charge configuration on the microtubule provides the guide for motion. Thus, while the chemical hydrolysis energy induces appropriate local conformational changes, the motor translational energy is fundamentally electrostatic. Numerical simulations of the mechanical equations of motion show that processivity and directionality are direct consequences of the ATP-dependent electrostatic interaction between the different charge distributions of kinesin and the microtubule. |
|---|