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  • Adaptation  (1)
  • Biochemistry  (1)
  • Biological and Medical Physics, Biophysics  (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: 1432-2013
    Keywords: Adaptation ; Hypertrophy ; Irradiation ; Myosin heavy chain ; Satellite cells ; Skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The right extensor digitorum longus (EDL) muscle of growing male rats was overloaded by ablation of its synergist tibialis anterior (TA) muscle. Four weeks later, the overloaded muscle was heavier and contained larger type IIA, IIX and IIB fibres than either untreated contralateral muscle or control muscle from an untreated animal. The myonuclear-to-myoplasmic volume ratio was maintained in the overloaded muscle. Overloaded EDL muscle, previously subjected to a dose of irradiation sufficient to sterilise satellite cells, and EDL muscle which had been only irradiated, were significantly lighter and contained significantly smaller fibres than controls, though a significant amount of normal EDL muscle growth did occur following either treatment. The myonuclear-to-myoplasmic volume ratio of the irradiated muscles was smaller than in controls. Overloaded muscle, with or without prior irradiation, possessed a smaller proportion of fibres containing IIB myosin heavy chain (MHC) and a larger proportion of fibres containing IIA and IIX MHC; a significant percentage of these fibres coexpressed either type IIA and IIX MHC or type IIX and IIB MHC. Thus in the absence of satellite cell mitosis, muscles of young rats possess a limited capacity for normal growth but not for compensatory hypertrophy. Adaptations in MHC gene expression to chronic overload are completely independent of satellite cell activity.
    Type of Medium: Electronic Resource
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