Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: Revaluation Books, Exeter, Regno Unito
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Aggiungi al carrelloPaperback. Condizione: Brand New. 92 pages. 8.66x5.91x0.21 inches. In Stock.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: preigu, Osnabrück, Germania
EUR 44,00
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Aggiungi al carrelloTaschenbuch. Condizione: Neu. Inhibitor designing of mycolic acid precursor RmlA of M. Tuberculosis | Rani Mansuri (u. a.) | Taschenbuch | 92 S. | Englisch | 2017 | LAP LAMBERT Academic Publishing | EAN 9783330052727 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: Mispah books, Redhill, SURRE, Regno Unito
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Aggiungi al carrellopaperback. Condizione: New. NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing Mai 2017, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germania
EUR 49,90
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Aggiungi al carrelloTaschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This book consist of development of Mycobacterium tuberculosis inhibitors through insilico approach such as design of side chain analogues through combinatorial approach. The designed analogues have good ADMET properties and Lipinski's drug like criterion and may be used as newer candidate for Tuberculosis. Apart from development of analogues the 3D model of RmlA protein responsible for the formation of mycolic acid was built and various designed analogues were screened through it, that yielded few potential inhibitors against RmlA. 92 pp. Englisch.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: moluna, Greven, Germania
EUR 41,71
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Aggiungi al carrelloCondizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Mansuri RaniDr. Rani Mansuri has completed her M.S. and PhD. from NIPER,Hajipur and RMRI,PATNA, India. She is expertise in various Insilico work such as database designing and programming, Docking and Virtual screenin, molecular dyn.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing Mai 2017, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: buchversandmimpf2000, Emtmannsberg, BAYE, Germania
EUR 49,90
Quantità: 1 disponibili
Aggiungi al carrelloTaschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -This book consist of development of Mycobacterium tuberculosis inhibitors through insilico approach such as design of side chain analogues through combinatorial approach. The designed analogues have good ADMET properties and Lipinski's drug like criterion and may be used as newer candidate for Tuberculosis. Apart from development of analogues the 3D model of RmlA protein responsible for the formation of mycolic acid was built and various designed analogues were screened through it, that yielded few potential inhibitors against RmlA.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 92 pp. Englisch.
Lingua: Inglese
Editore: LAP LAMBERT Academic Publishing, 2017
ISBN 10: 3330052724 ISBN 13: 9783330052727
Da: AHA-BUCH GmbH, Einbeck, Germania
EUR 49,90
Quantità: 1 disponibili
Aggiungi al carrelloTaschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - This book consist of development of Mycobacterium tuberculosis inhibitors through insilico approach such as design of side chain analogues through combinatorial approach. The designed analogues have good ADMET properties and Lipinski's drug like criterion and may be used as newer candidate for Tuberculosis. Apart from development of analogues the 3D model of RmlA protein responsible for the formation of mycolic acid was built and various designed analogues were screened through it, that yielded few potential inhibitors against RmlA.