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    Wyświetlanie 1-2 z 2
    Tytuł:
    Geophysical mapping for structural geology, prospecting and environment
    Autorzy:
    Gajewski, A.
    Szczypa, S.
    Wójcicki, A.
    Powiązania:
    https://bibliotekanauki.pl/articles/2065884.pdf
    Data publikacji:
    2005
    Wydawca:
    Państwowy Instytut Geologiczny – Państwowy Instytut Badawczy
    Tematy:
    geophysical mapping
    structural recognition
    geophysical prospecting
    soil pollution
    groundwater pollution
    groundwater monitoring
    Opis:
    Applications of geophysical mapping to structural geology, prospecting and environment protection purposes are presented. Both classic and more advanced geophysical methods can be employed to enhance either regional, semi-detailed or detailed mapping of geological structures. In the case of regional and semi-detailed studies, gravity and magnetotelluric methods are supplementary to seismic, especially where significant screening and attenuating of seismic waves occur. Detailed investigations of environmental protection issues might include a wide range of geophysical methods, but in the case of investigation of groundwater pollution usually resistivity methods are applied. Examples of geophysical works performed by the PBG Geophysical Exploration Company illustrate these applications.
    Źródło:
    Przegląd Geologiczny; 2005, 53, 10/2; 973--976
    0033-2151
    Pojawia się w:
    Przegląd Geologiczny
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structure-function relationship of serine protease-protein inhibitor interaction.
    Autorzy:
    Otlewski, Jacek
    Jaskólski, Mariusz
    Buczek, Olga
    Cierpicki, Tomasz
    Czapińska, Honorata
    Krowarsch, Daniel
    Smalas, Arne
    Stachowiak, Damian
    Szpineta, Agnieszka
    Dadlez, Michał
    Powiązania:
    https://bibliotekanauki.pl/articles/1044133.pdf
    Data publikacji:
    2001
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calorimetry
    serine proteases
    structural thermodynamics
    protein inhibitor
    protein-protein recognition
    Opis:
    We report our progress in understanding the structure-function relationship of the interaction between protein inhibitors and several serine proteases. Recently, we have determined high resolution solution structures of two inhibitors Apis mellifera chymotrypsin inhibitor-1 (AMCI-I) and Linum usitatissimum trypsin inhibitor (LUTI) in the free state and an ultra high resolution X-ray structure of BPTI. All three inhibitors, despite totally different scaffolds, contain a solvent exposed loop of similar conformation which is highly complementary to the enzyme active site. Isothermal calorimetry data show that the interaction between wild type BPTI and chymotrypsin is entropy driven and that the enthalpy component opposes complex formation. Our research is focused on extensive mutagenesis of the four positions from the protease binding loop of BPTI: P1, P1', P3, and P4. We mutated these residues to different amino acids and the variants were characterized by determination of the association constants, stability parameters and crystal structures of protease-inhibitor complexes. Accommodation of the P1 residue in the S1 pocket of four proteases: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 variants. High resolution X-ray structures of ten complexes between bovine trypsin and P1 variants of BPTI have been determined and compared with the cognate P1 Lys side chain. Mutations of the wild type Ala16 (P1') to larger side chains always caused a drop of the association constant. According to the crystal structure of the Leu16 BPTI-trypsin complex, introduction of the larger residue at the P1' position leads to steric conflicts in the vicinity of the mutation. Finally, mutations at the P4 site allowed an improvement of the association with several serine proteases involved in blood clotting. Conversely, introduction of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing effect on the complex with these proteases.
    Źródło:
    Acta Biochimica Polonica; 2001, 48, 2; 419-428
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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