منابع مشابه
Light meromyosin paracrystal formation
STUDIES OF PARACRYSTAL FORMATION BY COLUMN PURIFIED LIGHT MEROMYOSIN (LMM) PREPARED IN A VARIETY OF WAYS LED TO THE FOLLOWING CONCLUSIONS: (a) different portions of the myosin rod may be coded for different stagger relationships. This was concluded from observations that paracrystals with different axial repeat periodicities could be obtained either with LMM framents of different lengths prepar...
متن کاملThe light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever.
Structural data led to the proposal that the molecular motor myosin moves actin by a swinging of the light chain binding domain, or "neck." To test the hypothesis that the neck functions as a mechanical lever, smooth muscle heavy meromyosin (HMM) mutants were expressed with shorter or longer necks by either deleting or adding light chain binding sites. The mutant HMMs were characterized kinetic...
متن کاملMutations of the light meromyosin domain of the beta-myosin heavy chain rod in hypertrophic cardiomyopathy.
Familial hypertrophic cardiomyopathy (HCM) is caused by mutations in 9 sarcomeric protein genes. The most commonly affected is beta-myosin heavy chain (MYH7), where missense mutations cluster in the head and neck regions and directly affect motor function. Comparable mutations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly...
متن کاملThe axial repeats in paracrystals of light meromyosin and its complex with C-protein.
We examined the axial repeats in electron micrographs of three types of negatively stained paracrystals (two tactoid- and one sheet-like type) of rabbit light meromyosin (LMM) and its complex with C-protein characterized previously by similar axial period of about 43.0 nm. Assuming for the axial repeat in type II tactoids the value of 42.93 +/- 0.05 nm as it was determined by X-ray diffraction ...
متن کاملExpression of light meromyosin in Dictyostelium blocks normal myosin II function
The ability of myosin II to form filaments is essential for its function in vivo. This property of self association is localized in the light meromyosin (LMM) region of the myosin II molecules. To explore this property in more detail within the context of living cells, we expressed the LMM portion of the Dictyostelium myosin II heavy chain gene in wild-type Dictyostelium cells. We found that th...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1971
ISSN: 0002-1369
DOI: 10.1080/00021369.1971.10860059