The Research Of Magnetization Dynamics Under A Spin Polarization Current

Conventional kinesin’s neck linker(NL) docking to the motor domain is one of the key force generation processes of this molecular machine. In the initiation step of the NL docking process the first three amino acids(LYS325, THR326 and ILE327 in 2KIN) of NL must form an “extra turn” structure so that the other parts of NL could dock to the motor domain consecutively. Experiments have revealed that NL docking can only be initiated by ATP binding. Therefore, the extra turn formation mechanism of NL’s first three amino acids is a key point for understanding kinesin’s mechanochemical cycling. Using molecular dynamics simulation we investigate the extra turn formation mechanism based on a detailed analysis of the structure and the related interactions. We find that the motor head rotation induced by ATP binding can drive ILE327 move towards the hydrophobic pocket in the motor domain. The corresponding driving force, together with the hydrophobic interaction between ILE327 and the hydrophobic pocket, causes a clockwise rotation of THR326, breaks the locking function of LYS325 and, finally, drives the formation of the extra turn. This extra turn formation process provides a clear pathway from ATP binding to NL docking on kinesin and is thus a key step for achieving motility in life.