ArticleBiophysical journal2001
Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Effect of N-Terminal Extension of Cardiac Troponin I on the Ca(2+) Regulation of ATP Binding and ADP Dissociation of Myosin II in Native Cardiac Myofibrils.Biochemistry · 2016Article
- Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin.The Journal of biological chemistry · 2009Article
- Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates.The Journal of physiology · 2005Article
- Longitudinal distortions and transversal fluctuations of an actin filament sliding on Myosin molecules.Journal of biological physics · 2002Article
- Effects of substituting uridine triphosphate for ATP on the crossbridge cycle of rabbit muscle.The Journal of physiology · 2001Article
- The path to visualization of walking myosin V by high-speed atomic force microscopy.Biophysical reviewsArticle
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have attempted to link the solution actomyosin ATPase with the mechanical properties of in vitro actin filament sliding over heavy meromyosin. To accomplish this we perturbed the system by altering the substrate with various NTPs and divalent cations, and by altering ionic strength. A wide variety of enzymatic and mechanical measurements were made under very similar solution conditions. Excellent correlations between the mechanical and enzymatic quantities were revealed. Analysis of these correlations based on a force-balance model led us to two fundamental equations, which can be described approximately as follows: the maximum sliding velocity is proportional to square root of V(max)K(m)(A), where K(m)(A) is the actin concentration at which the substrate turnover rate is half of its maximum (V(max)). The active force generated by a cross-bridge under no external load or under a small external load is proportional to square root of V(max)/K(m)(A). The equations successfully accounted for the correlations observed in the present study and observations in other laboratories.
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