Single kinesin molecules studied with a molecular force clamp

Article Abstract:

A number of new features have been highlighted by analysis of records of kinesin motion under variable ATP concentrations and loads. The discovery of tight coupling between ATP hydrolysis and mechanical stepping would appear to discount many existing theoretical models for force generation by kinesin. The kinesin stall force is determined by the ATP concentration, while raised loads reduce the maximum velocity and boost the apparent Michaelis-Menten constant.

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Kinesin hydrolyses one ATP per 8-nm step

Article Abstract:

The two-headed ATP dependent motor protein kinesin moves along microtubules in steps of 8 nm. The processivity of kinesin is used to determine the coupling ration to direct measurements of ATPase activity. Kinesin molecules were found to hydrolyse at single ATP molecule per 9-nm advance, based on statistical analysis and fluctuation studies.

Hydrolysis

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Doing a rotary two-step

Article Abstract:

Issues are presented concerning the use of molecular mechanics by organisms for the construction of molecular motors. The flow of energy in mechanisms which use ATP binding at a catalytic site is discussed.

Adenosine triphosphatase, Molecular microbiology

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