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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 229-236 
    ISSN: 0886-1544
    Keywords: α-helix ; filament motility ; filament contractility ; filament sliding ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The twisting behavior of α helices has hardly been considered hitherto with regard to the function of proteins. The well-known electrostatic repulsion between the highly charged side chains, which depends on their interaction with ions, is absolutely connected with torsional rotations of the helix as long as its hydrogen bonds hold. This means a direct transformation of chemical into mechanical energy. However, the stability of a twisted single α helix with charged side chains is low in an aqueous environment. It may easily ball up to form a globular molecule with nonhelical regions of the polypeptide chain. This corresponds to a primitive contraction that obviously occurs with spasminlike proteins that contain strongly twisted filaments as Salisbury [J. Submicrosc. Cytol. 15:105-110, 1983] has shown. Steps that increase the stability and rigidity of α helical filaments are (1) the formation of coiled-coils, (2) self-intertwining (“telephone cord phenomenon”) or intertwining with other coiled-coils as shown with the intermediate filaments, and (3) association with cytoskeletal elements (microfilaments, protofilaments of microtubules) that contain globular subunits. These coarser elements are rotated by winding and unwinding of the smaller helical molecules and thus transmit the torsion produced in the α helices to the microscopic level by the sliding (screwing) motion and the shearing effect that is connected with the waves of a rotating helix. Particles are transported if connected to the helical side arms. Since the displacement of the side arms seems to occur along the single protofilaments of a microtubule, a rotation of these protofiiaments is suggested. The bidirectional transport of particles along single microtubules may be explained by the association of left- and right-handed helices with the protofilaments. According to the models, parallel and antiparallel sliding of neurofilaments and neurotubules is suggested.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1981), S. 371-385 
    ISSN: 0886-1544
    Keywords: rotating filaments ; cytoplasmic streaming ; Nitella ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Our knowledge about the actin-containing characean filaments on the basis of light and electron microscopical investigations is reviewed. Dynamic filamentous networks, known already from isolated droplets, were detected in Nitella rhizoidal cells using light microscopical techniques. Earlier light microscopic observations in cytoplasmic droplets are confirmed and complemented by new model experiments with rotating helices. The motile phenomena occurring at the filament bundles (ring formation, wave propagation, particle translocation, net dynamics, rolling motions, formation of side arms) can, in this way, be imitated in detail. Thus, the concept of cytoplasmic streaming as a translocation along bundles of rapidly rotating helical filaments is supported. In order to explain unidirectional cytoplasmic streaming, a periodic winding up and unwinding of fine filaments is postulated by which ions are periodically bound and displaced. The formation of side arms which is favored during unwinding results in a screw-mechanical different behavior of the filaments in the two directions of rotation and therefore causes permanent particle transport in one direction.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 209-216 
    ISSN: 0886-1544
    Keywords: uniplanar flagella ; doublet microtubules ; doublet interaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The structural and mechanical properties of the helix-shaped isolated doublet microtubules described by Costello [Biol. Bull. 145:279-291, 1973], Zobel [J. Cell Biol. 59:573-94, 1973], and Miki-Noumura and Kamiya [Exp. Cell Res. 97:451-53, 1976, J. Cell Biol 81:355-60, 1979] are simulated by a left-handed superhelix model that consists of two intertwined springlike helices with a slight difference in their pitches. It is shown by combinations of two and more superhelices of this kind that the straight shape of the doublets in the axoneme is the consequence of a position-dependent mechanical coil-coil interaction between interconnected doublets whose curvatures bend against one another. A counterclockwise torsion changes the sense of the superhelix from the left-handed form with a smaller pitch (L2) to the right-handed form with a larger pitch (R3). The coil-coil interaction of L helices with R helices results in uniplanar, meanderlike shapes or in flattened helices. The one-sided distribution of L and R doublets as described for sperm axonemes by Costello [Biol. Bull. 145:279-91, 1973] may therefore be responsible for the uniplanar. meanderlike shape of these flagella.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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