Statistical determination of the step size of molecular motors

Publication Type:

Journal Article

Source:

JOURNAL OF PHYSICS-CONDENSED MATTER, IOP PUBLISHING LTD, Volume 17, Number 47, Sp. Is, DIRAC HOUSE, TEMPLE BACK, BRISTOL BS1 6BE, ENGLAND, p.S3811-S3820 (2005)

DOI:

10.1088/0953-8984/17/47/012

Keywords:

FLUCTUATION ANALYSIS; FORCE CLAMP; HELICASE; KINETICS; MECHANISM; MOTION; MOVEMENT; NOISE; SINGLE-STRANDED-DNA; TRANSLOCATION

Abstract:

Molecular motors are enzymatic proteins that couple the consumption of chemical energy to mechanical displacement. In order to elucidate the translocation mechanisms of these enzymes, it is of fundamental importance to measure the physical step size. The step size can, in certain instances, be directly measured with single-molecule techniques; however, in the majority of cases individual steps are masked by noise. The step size can nevertheless be obtained from noisy single-molecule records through statistical methods. This analysis is analogous to determining the charge of the electron from current shot noise. We review methods for obtaining the step size based on analysing, in both the time and frequency domains, the variance in position from noisy single-molecule records of motor displacement. Additionally, we demonstrate how similar methods may be applied to measure the step size in bulk kinetic experiments.