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    Tytuł:
    Thermodynamics of specific protein-RNA interactions.
    Autorzy:
    Stolarski, Ryszard
    Powiązania:
    https://bibliotekanauki.pl/articles/1043600.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calorimetry
    thermodynamics
    fluorescence
    proteins
    specific binding
    RNA 5' cap
    Opis:
    Description of the recognition specificity between proteins and nucleic acids at the level of molecular interactions is one of the most challenging tasks in biophysics. It is key to understanding the course and control of gene expression and to the application of the thus acquired knowledge in chemotherapy. This review presents experimental results of thermodynamic studies and a discussion of the role of thermodynamics in formation and stability of functional protein-RNA complexes, with a special attention to the interactions involving mRNA 5' cap and cap-binding proteins in the initiation of protein biosynthesis in the eukaryotic cell. A theoretical framework for analysis of the thermodynamic parameters of protein-nucleic acid association is also briefly surveyed. Overshadowed by more spectacular achievements in structural studies, the thermodynamic investigations are of equal importance for full comprehension of biopolymers' activity in a quantitative way. In this regard, thermodynamics gives a direct insight into the energetic and entropic characteristics of complex macromolecular systems in their natural environment, aqueous solution, and thus complements the structural view derived from X-ray crystallography and multidimensional NMR. Further development of the thermodynamic approach toward interpretation of recognition and binding specificity in terms of molecular biophysics requires more profound contribution from statistical mechanics.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 2; 297-318
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Wiązanie jonów na granicy faz oraz specyficzne efekty jonowe
    Ion binding to interfaces and specific ion effects
    Autorzy:
    Jakubowska, A.
    Powiązania:
    https://bibliotekanauki.pl/articles/172482.pdf
    Data publikacji:
    2012
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    wiązanie jonów
    metody badawcze
    teorie i modele
    specyficzne efekty jonowe
    binding of ions
    research methods
    theories and models
    specific ion effects
    Opis:
    Many biological processes taking place across or at membrane surfaces depend on the interaction between interfaces and ions (derived from the background salt) [1]. Binding of ions to surfactant bilayers, nucleic acids, proteins, and biological membranes markedly affects their stability and properties [2–8]. There are different techniques to measure the ion binding to interfaces, including: nuclear magnetic resonance (NMR) spectroscopy [2, 18-20], the method based on measuring of electrophoretic mobility and the so-called zeta potential measurements [4, 21], the method based on measuring of a ratio of acid-to-base forms of the spectrophotometric indicator pyridine- 2-azo-p-dimethylaniline, PADA [12], and the chemical-trapping method [22]. The above-mentioned methods permit investigation of the binding of either cations or anions to interfaces. Many theories and models had been proposed to describe quantitatively the interactions and distribution of ions at a charged surface. The earliest one was proposed by Gouy and Chapman [23, 24]. However, the classical Gouy–Chapman theory was too simplified due to the neglect of the geometrical dimensions of the ions [27]. Other theories have been developed on the basis of the Poisson–Boltzmann theory and the Poisson–Boltzmann equation (equation 3). This equation has been modified by an introduction of different terms [25, 42]. Recently, Radke et al. proposed interesting models of the ion distribution near the interface: the ion binding model [28] (Fig. 1) and the ion image charge interaction model [51] (Fig. 3). Interaction and binding of ions with interfaces is related to the so-called specific ion effects arising at exchanging ions of the same valence. Franz Hofmeister, Professor of Pharmacology at the University of Prague was the first who studied these effects systematically [13, 14]. The specific ion effects play a significant role in a wide range of biological and physicochemical phenomena from the salt solubility, electrolyte activities, the surface tension of electrolyte solutions, values of pH and zeta potentials, the buffer acting, microemulsion microstructure, cloud points of polymers and surfactant solutions to the action of ions on ion-channels in biological membranes (ion transport across membranes), in enzyme activities, in bacterial growth, and in the interaction between membranes [15, 16]. The biological cell activity is also connected to Hofmeister effects. The ion specificity observed is, in fact, a combination of different subtle effects, such as ion size, hydration of ions, ion effect on interfacial water structure, electrostatic and dispersion interactions, thermal motion, and fluctuations [26, 29–31]. Because of a combination of those different effects, Hofmeister effects remain unexplained by the present theories of physical chemistry [16].
    Źródło:
    Wiadomości Chemiczne; 2012, 66, 3-4; 193-208
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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