Auto-Inhibition of Actin-Myosin Atpase through Collective Force Generation
نویسندگان
چکیده
منابع مشابه
High-speed atomic force microscopy of protein dynamics: myosin on actin and rotary enzyme F1-ATPase
AFM allows the visualization of biological samples under physiological solution conditions, at high spatial resolution. However, captured images are limited to snapshots because it takes at least 30 seconds to capture an image, whereas biological phenomena are highly dynamic. To overcome this limitation, my group has developed high-speed AFM. The dynamic processes and structural dynamics of pro...
متن کاملInhibition of myosin ATPase by vanadate ion.
Inhibition of the myosin ATPase by vanadate ion (Vi) has been studied in 90 mM NaCl/5 mM MgCl2/20 mM Tris-HCl, pH 8.5, at 25 degrees C. Although the onset of inhibition during the assay is slow and dependent upon Vi concentration (kapp approximately 0.3 M-1 s-1), the final level of inhibition approaches 100%, provided the Vi concentration is in slight excess over the concentration of ATPase sit...
متن کاملInhibition of actin-activated myosin Mg(2+)-ATPase in smooth muscle by ruthenium red.
Ruthenium red was found to inhibit actin-activated myosin Mg(2+)-ATPase in smooth muscle and to bind to myosin heavy chain, but not to F-actin. The inhibition by Ruthenium red of actin-activated Mg(2+)-ATPase was of the competitive type with respect to actin (Ki 4.4 microM) and of the non-competitive type with respect to ATP (Ki 6.6 microM). However, Ruthenium red scarcely dissociated the acto-...
متن کاملCorrelation between calponin and myosin subfragment 1 binding to F-actin and ATPase inhibition.
Calponin is a thin-filament-associated protein that has been implicated in the regulation of smooth-muscle contractility. It binds to F-actin and inhibits the MgATPase activity of actomyosin. In the present work we have examined the effect of recombinant chicken gizzard alpha-calponin (R alpha CaP) on the binding of rabbit skeletal-muscle myosin subfragment 1 (S1) to F-actin and on the inhibiti...
متن کاملForce generation, but not myosin ATPase activity, declines with age in rat muscle fibers.
We tested the hypothesis that age-associated decline in muscle function is related to a change in myosin ATPase activity. Single, glycerinated semimembranosus fibers from young (8-12 mo) and aged (32-37 mo) Fischer 344 x Brown Norway male rats were analyzed simultaneously for force and myosin ATPase activity over a range of Ca2+ concentrations. Maximal force generation was ~20% lower in fibers ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2020
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2019.11.2442