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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
    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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  • 3
    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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  • 4
    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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  • 5
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Some 30 cytokine amino acid sequences (mainly interleukins, colony stimulating factors and tumor necrosis factors) have been examined for evidence of secondary structure as well as longer-range interactions of a type likely to lead to stable α-helical bundles. Most, though not all, of the cytokines examined have a high predicted α-helical content (40-60%) and quasi-repeating heptads containing i/i+3 apolar periodicities. This major subset of the cytokines is predicted to be characterized by molecules in which 4-α-helical bundles with an average length of 25Å are the most marked conformational features. Based on these conclusions, we suggest structures for huG-CSF, huGM-CSF and muIL-5 in which defined loop segments at the ends of helical bundles are the most likely sites for binding and recognition by specific cell receptors. As such, they provide a means for testing or refining the three working models we have defined, using currently available methods of site-directed substitution and deletion mutagenesis, as well as synthetic peptides corresponding to the proposed loop sequences and the use of monoclonal antibodies of defined epitopic specificity. The structure arrived at for huGM-CSF is consistent with the limited data currently available concerning the residues which are important for binding and activity.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Double ionization of the 1,1-dimethyl allene molecule to triplet electronic states of the dication has been studied using theoretical and experimental methods. Although the calculated data indicate a high density of states, suitable groupings of calculated double-ionization energies to those states agree well with values measured by double-charge-transfer spectroscopy. This indicates that the theoretical predictions provide an accurate indication of the composition of the triplet-state manifold for the 1,1-dimethyl allene dication between 25.2 eV and 39.6 eV.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    ISSN: 0020-7608
    Keywords: Chemistry ; Theoretical, Physical and Computational Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Double-ionization energies, for transitions from the ground state of the neutral propyne molecule to both singlet and triplet states of its dication, are investigated theoretically with the ab initio second-order algebraic diagrammatic construction [ADC(2)] propagator method. The results are compared with a previous study which reported both experimental data obtained from double-charge-transfer (DCT) spectroscopy and their analysis with semiempirical theory. The ADC(2) predictions match almost all the experimental peaks well. In the lower-energy range, for transitions to dication states up to 7 eV above the ground state, ADC(2) predictions indicate that significant energy separations of those dication terms dominated by a common electronic configuration are responsible for previous difficulties in the assignment of peaks in that region. At higher energies, both configuration interaction and satellite ionizations are significant.   © 1997 John Wiley & Sons, Inc. Int J Quant Chem 64: 175-182, 1997
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0887-3585
    Keywords: coiled-coli ; alpha-helix ; antiphagocytic ; heptad ; antigenic variation ; sequence repeats ; cell wall protein ; intermediate filaments ; myosin ; tropomyosin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: M protein is considered a virulence determinant on the streptococcal cell wall by virtue of its ability to allow the organism to resist attack by human neutrophils. The complete DNA sequence of the M6 gene from streptococcal strain D471 has allowed, for the first time, the study of the structural characteristics of the amino acid sequence of an entire M protein molecule. Predictive secondary structural analysis revealed that the majority of this fibrillar molecule exhibits strong alpha-helical potential and that, except for the ends, nonpolar residues in the central region of the molecule exhibit the 7-residue periodicity typical for coiled-coil proteins. Differences in this heptad pattern of nonpolar residues allow this central rod region to be divided into three subdomains which correlate essentially with the repeat regions A, B, and C/D in the M6 protein sequence. Alignment of the N-terminal half of the M6 sequence with PepM5, the N-terminal half of the M5 protein, revealed that 42% of the amino acids were identical. The majority of the identities were “core” nonpolar residues of the heptad periodicity which are necessary for the maintenance of the coiled coil. Thus, conservation of structure in a sequence-variable region of these molecules may be biologically significant. Results suggest that serologically different M proteins may be built according to a basic scheme: an extended central coiled-coil rod domain (which may vary in size among strains) flanked by functional end domains.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1076-5174
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Vertical double-ionization energies of ethylamine, propylamine and butylamine molecules to triplet electronic states of their dications were measured by double-charge-transfer spectroscopy. The energies to the lowest states of the dications were calculated using an ab initio method with four basis sets. The calculated values predicted fairly well the reduction in the lowest energy observed when the length of the substituted alkyl group increased. Double-ionization energies to the lowest and higher lying triplet states of the dications were calculated by application of a semi-empirical form of the multiple scattering Xα method. Even though several spectral peaks may only be identified with transitions to groups of closely lying states, the calculated data gave an insight into the electronic transitions which take place to give the double-charge-transfer spectra.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 10
    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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