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  • 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
    Call number: 04-ZELL:360a
    Keywords: Cytoplasmic filaments ; Filament / Intermediaer
    Pages: 183 p. : ill.
    ISBN: 1570591202
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    04-ZELL:360a departmental collection or stack – please contact the library
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  • 3
    ISSN: 1573-6881
    Keywords: Mitochondria ; hexokinase ; normal and tumor cells ; enzyme localization ; subcellular fractionation ; receptor for binding ; monoamine oxidase ; NADPH-cytochromec reductase ; transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Hexokinase plays an important role in normal glucose-utilizing tissues like brain and kidney, and an even more important role in highly malignant cancer cells where it is markedly overexpressed. In both cell types, normal and transformed, a significant portion of the total hexokinase activity is bound to particulate material that sediments upon differential centrifugation with the crude “mitochondrial” fraction. In the case of brain, particulate binding may constitute most of the total hexokinase activity of the cell, and in highly malignant tumor cells as much as 80 percent of the total. When a variety of techniques are rigorously applied to better define the particulate location of hexokinase within the crude “mitochondrial fraction,” a striking difference is observed between the distribution of hexokinase in normal and transformed cells. Significantly, particulate hexokinase found in rat brain, kidney, or liver consistently distributes with nonmitochondrial membrane markers whereas the particulate hexokinase of highly glycolytic hepatoma cells distributes with outer mitochondrial membrane markers. These studies indicate that within normal tissues hexokinase binds preferentially to non-mitochondrial receptor sites but upon transformation of such cells to yield poorly differentiated, highly malignant tumors, the overexpressed enzyme binds preferentially to outer mitochondrial membrane receptors. These studies, taken together with the well-known observation that, once solubilized, the particulate hexokinase from a normal tissue can bind to isolated mitochondria, are consistent with the presence in normal tissues of at least two different types of particulate receptors for hexokinase with different subcellular locations. A model which explains this unique transformation-dependent shift in the intracellular location of hexokinase is proposed.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4935
    Keywords: amino acid sequence ; paramyosin ; schistosome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The cDNA encoding about half of an antigenic non-surface schistosome parasite protein of M r 97 K has recently been cloned and sequenced (Lanar, Pearce, James and Sher (1986)Science 234:593–596). Analysis of this sequence, together with the properties of the native protein, reveals that this protein is paramyosin, the hitherto unsequenced core protein of myosin filaments in invertebrate muscle. In this report we analyze in more detail the partial amino acid sequence of schistosome paramyosin and describe electron microscope studies of the native protein and its aggregates. We show a close correspondence between the structures of paramyosin and the myosin rod that is required for these proteins to assemble together in muscle thick filaments.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-2568
    Keywords: sarcoidosis ; hyperlipasemia ; pancreatic sarcoid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Double-charge-transfer spectroscopy is routinely used to measure double-ionization energies of molecules to singlet and triplet electronic states of dications, but is experimentally difficult to apply because the yield of negative ions generated in the double-electron-capture reactions is low. The use of a data-acquisition system and repetitive scanning of a spectrum can increase signal-to-noise ratios, but the number of scans that can be acquired is limited by drifting in the spectrum position, which results in spectral-peak broadening. This limitation has been overcome in the present investigation by the application of a computer enhancement program that effectively superimposes successive spectra which are subject to slight drift. Spectra obtained for H+ projectile ions reacting with hexafluorobenzene (C6F6) molecules are presented; use of the program with such spectra reveals features in the computer-enhanced spectrum which are not clearly evident in the individual spectra.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 4 (1991), S. 63-75 
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The amino acid sequences of human and murine haemopoietins have been analysed using algorithms predictive for secondary structure. The results for 19 of these proteins (human and murine Interleukins 2, 3, 4, 5, 6, 7 and granulocyte, macrophage and granulocyte macrophage-colony stimulating factors as well as human erythropoietin) suggest that they each contain a 4-α-helical bundle, ca 25 Å long, as a common conformational feature. The most important predictive indicator was considered to be occurrence of quasi-repeating sequences of seven amino acids of the form (a-b-c-d-e-f-g)n with a polar side chains (usually leucine) lying alternately three and four residues apart in the a and d positions. As with other proteins of known secondary structure this periodicity favors the formation of α-helical elements, each with an a polar external strip, which interdigitate closely with one another when tested appropriately. Molecular models based on these putative 4-α-helical bundles are presented - with special references to human granulocyte macrophage-colony stimulating factor. The extent to which such models are consistent with experiments designed to delineate receptor binding sites is discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0098-1273
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The results of extended Huckel calculations are reported for an isolated (SN)x chain in which some of the S2N2 units of the extended one-dimensional chain are replaced by (SCH2)2 units. It is found that, inter alia, the metallic behavior of the unsubstituted parent is retained but that the conductivity is lowered to an extent governed by the nature and degree of substitution.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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