Evidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil.

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Evidence that the stalk of Drosophila kinesin heavy chain is an alpha- helical coiled coil

Kinesin is a mechanochemical enzyme composed of three distinct domains: a globular head domain, a rodlike stalk domain, and a small globular tail domain. The stalk domain has sequence features characteristic of alpha-helical coiled coils. To gain insight into the structure of the kinesin stalk, we expressed it from a segment of the Drosophila melanogaster kinesin heavy chain gene and purified i...

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Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues. A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and chara...

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Helix-Coil Transitions of a-Helical, Two-Chain, Coiled Coils

A theory of the helix-coil transition for in-register, two-chain, a-helical, coiled coils such as tropomyosin and paramyosin is developed. The treatment differs from those formulated previously for DNAor collagen-like double helices; in the present treatment, isolated single chains and each of the two strands in the dimer may be partially helical. We calculate the fraction of helix in the two-c...

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Photoinduced electron-transfer along alpha-helical and coiled-coil metallopeptides.

A peptide-based electron-transfer system has been designed in which the specific positions of redox-active metal complexes appended to either an alpha-helix, or an alpha-helical coiled-coil, can be reversed to test the effect of the helix dipole in controlling photoinduced electron-transfer rates. Two 30-residue apopeptides were prepared having the following sequences: (I) Ac-K-(IEALEGK)(ICALEG...

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The coiled-coil helix in the neck of kinesin.

Kinesin is a microtubule-dependent motor protein. We have recently determined the X-ray structure of monomeric and dimeric kinesin from rat brain. The dimer consists of two motor domains, held together by their alpha-helical neck domains forming a coiled coil. Here we analyze the nature of the interactions in the neck domain (residues 339-370). Overall, the neck helix shows a heptad repeat (abc...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1992

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.116.4.957