𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The tail of myosin reduces actin filament velocity in the in vitro motility assay

✍ Scribed by Guo, Bin ;Guilford, William H.

Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
192 KB
Volume
59
Category
Article
ISSN
0886-1544

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Actin-filament motion in the in vitro mo
Actin-filament motion in the in vitro motility assay has a periodic component
✍ deBeer, Evert L. ;Sontrop, Annemiek M.A.T.A. ;Kellermayer, Miklos S.Z. ;Galambos πŸ“‚ Article πŸ“… 1997 πŸ› John Wiley and Sons 🌐 English βš– 183 KB

The interaction between actin and myosin can be studied in the in vitro motility assay, where fluorescently labelled actin filaments are observed to move over a lawn of myosin heads. To examine details of this movement, we measured systematically the velocities of the front end, rear end, and centro

Path Reconstruction as a Tool for Actin
Path Reconstruction as a Tool for Actin Filament Speed Determination in the in Vitro Motility Assay
✍ W. Hamelink; J.G. Zegers; B.W. Treijtel; T. BlangΓ© πŸ“‚ Article πŸ“… 1999 πŸ› Elsevier Science 🌐 English βš– 88 KB

The in vitro motility assay is used to measure speed of actin filaments moving over a glass surface coated with heavy meromyosin. In this paper a new method, the path reconstruction method, is presented to evaluate observed speeds. The method is compared with the commonly used centroid method, in wh

In vitro motilities of the unconventiona
In vitro motilities of the unconventional myosins, brush border myosin-I, and chick brain myosin-V exhibit assay-dependent differences in velocity
✍ Wolenski, Joseph S. ;Cheney, Richard E. ;Forscher, Paul ;Mooseker, Mark S. πŸ“‚ Article πŸ“… 1993 πŸ› John Wiley and Sons 🌐 English βš– 814 KB

## Abstract Two types of in vitro motility assays are currently used for examining the mechanochemical properties of purified myosins. The __Nitella__ bead movement assay (Sheetz and Spudich: __Nature__ 303:31–35, 1983) allows determination of both velocity and directionality of movement, but is of

A Protein Friction Model of the Actin Sl
A Protein Friction Model of the Actin Sliding Movement generated by Myosin in Mixtures of MgATP and MgGTP in vitro
✍ Yasuhiro Imafuku; Yumiko Emoto; Katsuhisa Tawada πŸ“‚ Article πŸ“… 1999 πŸ› Elsevier Science 🌐 English βš– 220 KB

The sliding movement of an actin "lament generated by myosin heads with MgGTP bound is much slower than that by those with MgATP bound. Nonetheless, there is a report that the actin sliding velocity at low (11}21 M) MgATP concentrations is increased by the addition of MgGTP in a range of 1}3 mM, alt