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Wyszukujesz frazę "ligand-protein interaction" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
An approach based on diffusion to study ligand-macromolecule interaction.
Autorzy:
Housaindokht, Mohammad
Bahrololoom, Mahmood
Tarighatpoor, Shirin
Mossavi-Movahedi, Ali
Powiązania:
https://bibliotekanauki.pl/articles/1043738.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
binding isotherm
methyl orange
ligand-protein interaction
hen egg-white lysozyme
Opis:
A new approach has been developed to study binding of a ligand to a macromolecule based on the diffusion process. In terms of the Fick's first law, the concentration of free ligand in the presence of a protein can be determined by the measurement of those ligands which are diffused out. This method is applied to the study of binding of methyl-orange to lysozyme in phosphate buffer of pH 6.2, at 30°C. The binding isotherm was determined initially, followed by application of the Hill equation to the data obtained, then binding constant and binding capacity were estimated.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 703-707
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Electrostatics in computer-aided drug design
Autorzy:
Naray-Szabo, G.
Matyus, P.
Powiązania:
https://bibliotekanauki.pl/articles/1953955.pdf
Data publikacji:
1998
Wydawca:
Politechnika Gdańska
Tematy:
electrostatics
drug design
molecular electrostatic potential
molecular electrostatic field
similarity
pharmacophore
ComFa method
protein-ligand interaction
Opis:
Hydrogen bonds and charge-charge interactions, determined by molecular electrostatics, play essential role in biopolymer-ligand associations. Accordingly, electrostatics is crucial in the qualitative and quantitative characterisation of the binding of drugs to their target molecules. In the following, we will give an account on the role of molecular electrostatics in a drug design, laying emphasis on our own work. We will survey the most important computation methods of molecular electrostatic potentials, then outline basic aspects of molecular recognition: steric, electrostatic and hydrophobic complementarity. On the basis of the complementarity, we will also define molecular similarity and discuss various applications of these concepts to the treatment of protein-ligand interactions and a rational drug design. Special attention will be paid to a receptor mapping and to a comparative molecular field analysis, with some our recent applications. A further important point will be the molecular electrostatic field (potential gradient) as a hydrophobicity measure. We will argue that the hydrophobic complementarity and similarity can be treated on the basis of matching regions of the interacting molecules that are characterised by a similar magnitude of the electrostatic field. The concept of the electrostatic complementarity will be extended to enzyme-substrate interactions, providing a firm basis for the quantitative estimation of catalytic rate enhancement.
Źródło:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 1998, 2, 4; 551-562
1428-6394
Pojawia się w:
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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