Force production by single kinesin motors

Motor proteins such as kinesin, myosin and polymerase convert chemical ener gy into work through a cycle that involves nucleotide hydrolysis. Kinetic r ates in the cycle that depend upon load identify transitions at which struc tural changes, such as power strokes or diffusive motions, are likely to oc cur. Here we show, by modelling data obtained with a molecular force clamp, that kinesin mechanochemistry can be characterized by a mechanism in which a load-dependent isomerization follows ATP binding. This model quantitativ ely accounts for velocity data over a wide range of loads and ATP levels, a nd indicates that movement may be accomplished through two sequential 4-nm substeps. Similar considerations account for kinesin processivity, which is found to obey a load-dependent Michaelis-Menten relationship.