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  • Key words: Protein evolution — Trypsin — Tandem gene duplication — Fourier transform — Repeated segment  (1)
  • energy conservation  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pure and applied geophysics 144 (1995), S. 769-801 
    ISSN: 1420-9136
    Keywords: Hokkaido Nansei-Oki ; tsunami ; finite element modeling ; energy conservation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract A fault plane model and a finite element hydrodynamic model are applied to the simulation of the Hokkaido Nansei-Oki tsunami of July 12, 1993. The joint performance of the models is assessed based on the overall ability to reproduce observed tsunami waveforms and to preserve mass and energy during tsunami propagation. While a number of observed characteristics of the waveforms are satisfactorily reproduced (in particular, amplitudes and arrival times at tidal gauges relatively close to the source, and general patterns of energy concentration), others are only marginally so (notably, wave periods at the same gauges, and wave heights along Okushiri); differences between observations and simulations are traceable to both the fault plane and the hydrodynamic models. Nonnegligible losses of energy occur throughout the simulated tsunami propagation. These losses seem to be due to a combination of factors, including numerical damping and possible deficiencies of the shallow water equations in preserving energy.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 47 (1998), S. 353-362 
    ISSN: 1432-1432
    Keywords: Key words: Protein evolution — Trypsin — Tandem gene duplication — Fourier transform — Repeated segment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The trypsin family of serine proteases is one of the most studied protein families, with a wealth of amino acid sequence information available in public databases. Since trypsin-like enzymes are widely distributed in living organisms in nature, likely evolutionary scenarios have been proposed. A novel methodology for Fourier transformation of biological sequences (FOTOBIS) is presented. The methodology is well suited for the identification of the size and extent of short repeats in protein sequences. In the present paper the trypsin family of enzymes is analyzed with FOTOBIS and strong evidence for tandem gene duplication is found. A likely evolutionary path for the development of present-day trypsins involved an intrinsic extensive tandem gene duplication of a small DNA fragment of 15–18 nucleotides, corresponding to five or six amino acids. This ancestral trypsin gene was subsequently duplicated, leading to the earliest version of a full-sized trypsin, from which the contemporary trypsins have developed.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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