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dc.contributor.authorBOUACHA, IMADEDDINE-
dc.contributor.authorDJILALI BELOUFA, REDA-
dc.date.accessioned2024-03-04T08:40:01Z-
dc.date.available2024-03-04T08:40:01Z-
dc.date.issued2023-
dc.identifier.citationhttps://theses.univ-temouchent.edu.dz/opac_css/doc_num.php?explnum_id=5218en_US
dc.identifier.urihttp://dspace.univ-temouchent.edu.dz/handle/123456789/2816-
dc.description.abstractThe knowledge of the enzymes is capital, because it is catalyze the majority of the chemical reactions of the living organisms. The deterioration of the enzymes by specific inhibiters makes it possible to block the biochemical ways, only a particular site of enzymatic protein comes into contact with its substrate: it is the active site; this one is still divisible in two particular areas. The site can fixing; it possible the enzyme “to cling” to the molecule, and to position the latter in an optimal way, while the catalytic site starts the reactional process. Our work consists with a study of molecular interaction between 2BNH and the substrates, the various molecular numerical models are used to conclude this work (mechanical molecular, dynamic molecular and docking molecular) or the docking makes it possible to envisage how a small molecule (drug) can bind to a receiver (protein) of which the structure 3D is knowen_US
dc.subjectinteraction (enzyme-substrate), conformations, molecular modelingen_US
dc.titleANALYSE DE L’INTERACTION RIBONUCLÉASEANTIIBIOTIQUES PAR MODÉLISATION MOLÉCULAIREen_US
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