Evidence for flexibility of the helical rod section of the myosin molecule
| Autor: | Micheal Young, Murray Vernon King |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
Chemistry
Myosin Subfragments Muscle Proteins Torsion (mechanics) macromolecular substances Myosins Curvature Tail region Molecular physics Elasticity Models Structural Microscopy Electron Crystallography chemistry.chemical_compound Structural Biology Myosin Molecule Cyanogen bromide Cyanogen Bromide Molecular Biology Striation |
| Zdroj: | Journal of Molecular Biology. 65:519-523 |
| ISSN: | 0022-2836 |
| Popis: | Light meromyosin-C, a fragment from the tail region of myosin prepared by cyanogen bromide cleavage, yields, under suitable conditions, an aggregate having the form of hollow tubes. Both the inclined striation patterns of these tubes and the existence of oblique paths of easy cleavage indicate that the molecules of light meromyosin-C follow helical arcs in these aggregates. From specimen to specimen, the molecular arcs vary widely in their inclination to the tube axes. Thus, they vary also in their radii of torsion and curvature. These data indicate not only that the tail of the myosin molecule is flexible, but also that its equilibrium configuration under certain conditions is non-linear, a situation of some importance in devising models for the thick filament. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|