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  • α-fibrous proteins  (2)
  • Biochemistry  (1)
  • Gene Expression  (1)
  • Life sciences  (1)
  • 1
    Keywords: Life sciences ; Gene Expression ; Proteins ; Life sciences ; Protein Science ; Gene Expression ; Biological and Medical Physics, Biophysics ; Springer eBooks
    Description / Table of Contents: Fibrous Protein Structures: Hierarchy, History and Heroes -- Coiled-coil design: updated and upgraded -- Functional and Structural Roles of Coiled Coils -- The Structure and Topology of α-Helical Coiled Coils -- Structural Transition of Trichocyte Keratin Intermediate Filaments During Development in the Hair Follicle -- Crystallographic studies of intermediate filament proteins -- Lessons from animal models of cytoplasmic intermediate filament proteins -- Filamentous Structure of Hard β-Keratins in the Epidermal Appendages of Birds and Reptiles -- Tropomyosin Structure, Function, and Interactions: A Dynamic Regulator -- Titin and Nebulin in Thick and Thin Filament Length Regulation -- Myosin and Actin Filaments in Muscle: Structures and Interactions -- Dystrophin and spectrin, two highly dissimilar sisters of the same family -- Fibrin Formation, Structure and Properties -- Fibrillar collagens -- Recombinant structural proteins and their use in future materials -- Properties of engineered and fabricated silks -- Biomaterials Made from Coiled Coil Peptides -- Bioengineered Collagens
    Abstract: This book provides the readers with an up-to-date review of the design, structure and function of a representative selection of fibrous proteins in both health and disease. The importance of the α-helical coiled coil, a conformational motif based on the heptad repeat in the amino acid sequence of all α-fibrous proteins (and parts of some globular proteins) is underlined by three Chapters devoted to its design, structure, function and topology. Specific proteins covered in the text and which depend on the coiled coil for their structure and function, include the intermediate filament proteins, tropomyosin, myosin, paramyosin, fibrin and members of the spectrin superfamily. Also described are fibrous proteins based on the β-pleated sheet and collagen conformations. Recombinant structural proteins, especially of silk and collagen, are discussed in the context of developing new biomaterials with varied applications. Established researchers and postgraduate students in the fields of protein chemistry, biochemistry and structural biophysics will find Fibrous Proteins: Structures and Mechanisms to be an invaluable collection of topical reviews that describe the basic advances made in the field of fibrous proteins over the past decade. This book, written by recognized authorities in the field, provides a clear account of the current status of fibrous protein research and, in addition, establishes the basis for deciding the most appropriate directions for future activity, including the applications of protein engineering and the commercial exploitation of new biomaterials
    Pages: VIII, 629 p. 154 illus., 123 illus. in color. : online resource.
    ISBN: 9783319496740
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  • 2
    ISSN: 0192-8651
    Keywords: Computational Chemistry and Molecular Modeling ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Computer Science
    Notes: Ab initio calculations employing a standard double-zeta basis set augmented with various polarization functions have been used to investigate the lowest energy region of the ground-state potential energy surface of the formamide molecule. Hartree-Fock calculations with only d polarization functions on the nonhydrogen atoms located two stable minima, that with geometry distorted from planarity having slightly lower energy; only one stable minimum with planar structure is found when p polarization functions on the hydrogens are included. In contrast optimizations, which account approximately for the correlation energy using second-order Møller-Plesset perturbation theory consistently favor a single slightly nonplanar minimum energy geometry.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0887-3585
    Keywords: α-fibrous proteins ; 4-α-helix bundle ; membrane-spanning proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0887-3585
    Keywords: α-fibrous proteins ; supercoiling ; structure prediction ; hemagglutinin ; mannose-binding protein ; protein engineering ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The discontinuities found in heptad repeats of α-helical coiled-coil proteins have been characterized. A survey of 40 α-fibrous proteins reveals that only two classes of heptad breaks are prevalent: the stutter, corresponding to a deletion of three residues, and the newly identified “stammer,” corresponding to a deletion of four residues. This restriction on the variety of insertions/deletions encountered gives support to a unifying structural model, where different degrees of supercoiling accommodate the observed breaks. Stutters in the hemagglutinin coiled-coil region have previously been shown to produce an underwinding of the supercoil, and we show here how, in other cases, stammers would lead to overwinding. An analysis of main-chain structure also indicates that the mannose-binding protein, as well as hemagglutinin, contains an underwound coiled-coil region. In contrast to knobs-into-holes packing, these models give rise to non-close-packed cores at the sites of the heptad phase shifts. We suggest that such non-close-packed cores may function to terminate certain coiled-coil regions, and may also account for the flexibility observed in such long α-fibrous molecules as myosin. The local underwinding or overwinding caused by these specific breaks in the heptad repeat has a global effect on the structure and can modify both the assembly of the protein and its interaction properties. © 1996 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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