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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 17 (2000), S. 499-513 
    ISSN: 1434-6036
    Keywords: PACS. 36.20.Ey Conformation (statistics and dynamics) - 61.46.+w Clusters, nanoparticles, and nanocrystalline materials - 87.15.-v Biomolecules: structure and physical properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract: The classical isodesmic one-dimensional model for equilibrium polymerization is generalized in order to describe self-assembly in systems forming fibrils. The model was applied to peptide solutions forming -sheet tapes which can further aggregate into stacks of various thickness: double tapes and fibrils (several double tapes stacked together). We found that in some cases the model yields several step-like transitions as the concentration increases: first from monomers to single or double tapes, and then to fibrils. The abruptness of the first transition is controlled by the free energy penalty for transformation of a peptide from random coil to a straight -strand conformation (the latter is characteristic for tapes). If both single and double tapes are allowed, the length of the aggregates after the first transition can be very large with high scission energies. For very low energies of attraction between double tapes, the transition from double tapes to fibrils happens separately (above the first transition), and it is even more abrupt and produces extremely long fibrils. The theoretical findings are used to extract the characteristic molecular parameters for the self-assembly of the de novo peptide DN1 forming polymeric -sheets in water.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 17 (2000), S. 481-497 
    ISSN: 1434-6036
    Keywords: PACS. 36.20.Ey Conformation – 61.46.+w Clusters, nanoparticles, and nanocrystalline materials - 87.15.-v Biomolecules: structure and physical properties
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract: The problem of fibril (fibre) formation in chiral systems is explored theoretically being supported by experiments on synthetic de novo 11-mer peptide forming self-assembled -sheet tapes. Experimental data unambiguously indicate that the tapes form fibrils of nearly monodisperse thickness ca . 8-10 nm. Fibril formation and stabilisation are attributed to inter-tape face-to-face attraction and their intrinsic twist, correspondingly. The proposed theory is capable of predicting the fibril aggregation number and its equilibrium twist in terms of molecular parameters of the primary tapes. The suggested novel mechanism of twist stabilisation of finite aggregates (fibrils) is different to the well-known stabilisation of micelles in amphiphilic systems, and it is likely to explain the formation and stability of fibrils in a wide variety of systems including proteinaceous amyloid fibres, sickle-cell hemoglobin fibres responsible for HbS anemia, corkscrew threads found in chromonics in the presence of chiral additives and native cellulose microfibrillar crystallites. The theory also makes it possible to extract the basic molecular parameters of primary tapes (inter-tape attraction energy, helical twist step, elastic moduli) from the experimental data.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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