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    Wyświetlanie 1-2 z 2
    Tytuł:
    Contribution of the intra- and intermolecular routes in autocatalytic zymogen activation: application to pepsinogen activation
    Autorzy:
    Varón, Ramón
    Fuentes, Matilde
    García-Moreno, Manuela
    Garcìa-Sevilla, Francisco
    Arias, Enrique
    Valero, Edelmira
    Arribas, Enrique
    Powiązania:
    https://bibliotekanauki.pl/articles/1041258.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    intermolecular activation
    intramolecular activation
    autocatalysis
    enzyme kinetics
    proenzyme activation
    Opis:
    Taking as the starting point a recently suggested reaction scheme for zymogen activation involving intra- and intermolecular routes and the enzyme-zymogen complex, we carry out a complete analysis of the relative contribution of both routes in the process. This analysis suggests the definition of new dimensionless parameters allowing the elaboration, from the values of the rate constants and initial conditions, of the time course of the contribution of the two routes. The procedure mentioned above related to a concrete reaction scheme is extrapolated to any other model of autocatalytic zymogen activation involving intra- and intermolecular routes. Finally, we discuss the contribution of both of the activating routes in pepsinogen activation into pepsin using the values of the kinetic parameters given in the literature.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 2; 407-420
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    O kilku osobliwościach w oddziaływaniach molekuł
    On some pecularities of intermolecular and intramolecular interactions
    Autorzy:
    Piela, L.
    Powiązania:
    https://bibliotekanauki.pl/articles/172004.pdf
    Data publikacji:
    2011
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    globalna optymalizacja
    zwijanie białek
    oddziaływanie dipol-dipol
    choroba prionowa
    autokataliza
    global optimization
    protein folding
    dipole-dipole interaction
    prion disease
    autocatalysis
    Opis:
    The ground state electronic energy represents a complicated function of the nuclear coordinates. Even for relatively small molecules this function may have many minima in the corresponding "energy landscape", very often myriads of minima, each of them corresponding to a stable configuration of the nuclei. This is why predicting the lowest-energy conformation or configuration represents a formidable task. There were many attempts to solve this problem for protein molecules, for which it is believed their native conformation corresponds to the lowest free energy. The challenge to find this conformation from a given sequence of amino acids is known as a "second genetic code". In fact all of these attempts based on some smoothing of the energy landscape. In the article some of these smoothing techniques are described, from a generic one to those, which finally turned out to be highly successful in finding native structures of globular proteins. When discussing the contributions to the conformational energy the importance of the hydrophobic effect as well as of the electrostatic interactions has been stressed. In particular it turned out that the dipole moments of the NH and of the CO bonds in proteins functioning in nature are oriented to good accuracy along the local intramolecular electric field. Thanks to enormous effort of the protein folding community it is possible to design such amino acid sequences, which fold to the desired protein 3D structure. A certain reliable theoretical technique of protein folding has been used to study a possibility of conformational autocatalysis. It turned out that a small protein of 32 amino acids, with carefully predesigned amino acid sequence, exhibits indeed such an effect, which may be seen as a model of the prion disease propagation.
    Źródło:
    Wiadomości Chemiczne; 2011, 65, 11-12; 935-952
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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