Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Monophenols and Diphenols compounds are used as inhibitors and among these the some compounds exhibited significant inhibitory activities against the tyrosinase. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. The active site of the tyrosinase is the two copper ions as binding site. The metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Discovery Studio3.1 was utilized to investigate the conformation and binding affinities of our small molecules. The results indicate a possible mechanism for their anti-tyrosinase activity which may involve anability to chelate the copper atoms which are required for the catalytic activity of tyrosinase.
Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.
As a Bioinformatics postgraduate (MSc, MTech) Upendra Bhele has worked on various projects as chemoinformatics, pharmacoinformatics and docking studies. He has various research papers under his name
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Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Monophenols and Diphenols compounds are used as inhibitors and among these the some compounds exhibited significant inhibitory activities against the tyrosinase. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. The active site of the tyrosinase is the two copper ions as binding site. The metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Discovery Studio3.1 was utilized to investigate the conformation and binding affinities of our small molecules. The results indicate a possible mechanism for their anti-tyrosinase activity which may involve anability to chelate the copper atoms which are required for the catalytic activity of tyrosinase. 96 pp. Englisch. N° de réf. du vendeur 9783659463747
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Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Monophenols and Diphenols compounds are used as inhibitors and among these the some compounds exhibited significant inhibitory activities against the tyrosinase. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. The active site of the tyrosinase is the two copper ions as binding site. The metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Discovery Studio3.1 was utilized to investigate the conformation and binding affinities of our small molecules. The results indicate a possible mechanism for their anti-tyrosinase activity which may involve anability to chelate the copper atoms which are required for the catalytic activity of tyrosinase. N° de réf. du vendeur 9783659463747
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Vendeur : moluna, Greven, Allemagne
Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Bhele UpendraAs a Bioinformatics postgraduate (MSc, MTech) Upendra Bhele has worked on various projects as chemoinformatics, pharmacoinformatics and docking studies. He has various research papers under his nameCopper containing . N° de réf. du vendeur 5157665
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Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagne
Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Monophenols and Diphenols compounds are used as inhibitors and among these the some compounds exhibited significant inhibitory activities against the tyrosinase. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. The active site of the tyrosinase is the two copper ions as binding site. The metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Discovery Studio3.1 was utilized to investigate the conformation and binding affinities of our small molecules. The results indicate a possible mechanism for their anti-tyrosinase activity which may involve anability to chelate the copper atoms which are required for the catalytic activity of tyrosinase.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 96 pp. Englisch. N° de réf. du vendeur 9783659463747
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Vendeur : preigu, Osnabrück, Allemagne
Taschenbuch. Etat : Neu. Insilico Binding Studies of Phenolic Compounds With Tyrosinase | Vitiligo Is an Acquired Cutaneous Skin Disease Characterized By Declining Melanocyte Function and Depigmentation | Upendra Bhele | Taschenbuch | 96 S. | Englisch | 2013 | LAP LAMBERT Academic Publishing | EAN 9783659463747 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu. N° de réf. du vendeur 105514651
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