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• W2146156928 abstract "Recently, Block and coworkers [Visscher, K., Schnitzer, M. J., & Block, S. M. (1999) Nature (London) 400, 184–189 and Schnitzer, M. J., Visscher, K. & Block, S. M. (2000) Nat. Cell Biol. 2, 718–723] have reported extensive observations of individual kinesin molecules moving along microtubules in vitro under controlled loads, F = 1 to 8 pN, with [ATP] = 1 μM to 2 mM. Their measurements of velocity, V , randomness, r , stalling force, and mean run length, L , reveal a need for improved theoretical understanding. We show, presenting explicit formulae that provide a quantitative basis for comparing distinct molecular motors, that their data are satisfactorily described by simple, discrete-state, sequential stochastic models. The simplest ( N = 2)-state model with fixed load-distribution factors and kinetic rate constants concordant with stopped-flow experiments, accounts for the global ( V , F , L , [ATP]) interdependence and, further, matches relative acceleration observed under assisting loads. The randomness, r ( F ,[ATP]), is accounted for by a waiting-time distribution, ψ documentclass[12pt]{minimal} usepackage{amsmath} usepackage{wasysym} usepackage{amsfonts} usepackage{amssymb} usepackage{amsbsy} usepackage{mathrsfs} setlength{oddsidemargin}{-69pt} begin{document} begin{equation*}{mathrm{_{1}^{+}}}end{equation*}end{document} ( t ), [for the transition(s) following ATP binding] with a width parameter ν ≡ 〈t〉 2 /〈(Δ t ) 2 〉≃2.5, indicative of a dispersive stroke of mechanicity ≃0.6 or of a few (≳ν − 1) further, kinetically coupled states: indeed, N = 4 (but not N = 3) models do well. The analysis reveals: ( i ) a substep of d 0 = 1.8–2.1 nm on ATP binding (consistent with structurally based suggestions); ( ii ) comparable load dependence for ATP binding and unbinding; ( iii ) a strong load dependence for reverse hydrolysis and subsequent reverse rates; and ( iv ) a large (≳50-fold) increase in detachment rate, with a marked load dependence, following ATP binding." @default.
• W2146156928 created "2016-06-24" @default.
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• W2146156928 date "2001-06-26" @default.
• W2146156928 modified "2023-10-15" @default.
• W2146156928 title "Simple mechanochemistry describes the dynamics of kinesin molecules" @default.
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• W2146156928 doi "https://doi.org/10.1073/pnas.141080498" @default.
• W2146156928 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/35413" @default.
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