منابع مشابه
The structural and mechanochemical cycle of kinesin.
Kinesin is a microtubule-based motor protein that pulls vesicles or organelles towards the plus end of microtubules. Structural changes in the protein that drive motility are coupled to ATP binding and hydrolysis. Here, we attempt to integrate recent structural and kinetic results into a picture of the mechanochemical cycle of kinesin.
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At the latest count the myosin family includes 35 distinct groups, all of which have the conserved myosin motor domain attached to a neck or lever arm, followed by a highly variable tail or cargo binding region. The motor domain has an ATPase activity that is activated by the presence of actin. One feature of the myosin ATPase cycle is that it involves an association/dissociation with actin for...
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Regulation of cytoplasmic dynein's motor activity is essential for diverse eukaryotic functions, including cell division, intracellular transport, and brain development. The dynein regulator Lis1 is known to keep dynein bound to microtubules; however, how this is accomplished mechanistically remains unknown. We have used three-dimensional electron microscopy, single-molecule imaging, biochemist...
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Abstract: Nano- size alumina particles have been synthesized by mechanical activation of a dry powder mixture of AlCl3 and CaO. Mechanical milling of the above raw materials with the conditions adopted in this study resulted in the formation of a mixture consisting of crystalline CaO and amorphous aluminum chlorides phases. There was no sign of chemical reaction occurring during milling stag...
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Background: Members of the eukaryotic Hsp90 family function as important molecular chaperones in the assembly, folding and activation of cellular signaling in development. Two hsp90 genes, hsp90 alpha and hsp90 beta, have been identified in fish and homeothermic vertebrates but not in poikilothermic vertebrates. In the present study, the expression of hsp90 alpha and hsp90 beta genes in Xenopus...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2011
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.12.2780