Insilico analysis of xylanases from thermophilic bacteria als von
5 Angebote vergleichen

Bester Preis: 49,24 (vom 01.07.2017)
1
9783330082946 - Arabinda Ghosh: Insilico analysis of xylanases from thermophilic bacteria
Symbolbild
Arabinda Ghosh

Insilico analysis of xylanases from thermophilic bacteria (2017)

Lieferung erfolgt aus/von: Deutschland DE PB NW

ISBN: 9783330082946 bzw. 3330082941, in Deutsch, LAP Lambert Academic Publishing Jun 2017, Taschenbuch, neu.

Lieferung aus: Deutschland, Versandkostenfrei.
Von Händler/Antiquariat, Agrios-Buch [57449362], Bergisch Gladbach, Germany.
Neuware - Microorganisms produce enzymes which have the ability convert a given substrate into a desired product. Enzyme became essential components of industries and often called as biocatalyst. Maintaining enzymes and obtaining desired product is a costly affair. In order to overcome such short coming bioinformatics has entered into the field of industrial enzymology. In this study xylanases enzyme from different extremophilic bacteria was selected for which protein were built by homology modeling each of receptors bears partial structural similarity which was also highlighted by similar active site residues but were positioned at different locations. In silico binding affinity of these enzyme shows is multi-substrate activity and among the twenty amino acids Glutamate, Lysine, Arginine, Serine, Aspartic acid, Glutamine and Thereonine were found to be effective in binding to different type of ligands. 144 pp. Englisch.
2
9783330082946 - Arabinda Ghosh: Insilico analysis of xylanases from thermophilic bacteria
Arabinda Ghosh

Insilico analysis of xylanases from thermophilic bacteria (2017)

Lieferung erfolgt aus/von: Deutschland DE PB NW

ISBN: 9783330082946 bzw. 3330082941, in Deutsch, 144 Seiten, LAP Lambert Academic Publishing, Taschenbuch, neu.

Lieferung aus: Deutschland, Versandkosten nach: Deutschland, Versandkostenfrei.
Von Händler/Antiquariat, Sparbuchladen, [3602074].
Neuware - Microorganisms produce enzymes which have the ability convert a given substrate into a desired product. Enzyme became essential components of industries and often called as biocatalyst. Maintaining enzymes and obtaining desired product is a costly affair. In order to overcome such short coming bioinformatics has entered into the field of industrial enzymology. In this study xylanases enzyme from different extremophilic bacteria was selected for which protein were built by homology modeling each of receptors bears partial structural similarity which was also highlighted by similar active site residues but were positioned at different locations. In silico binding affinity of these enzyme shows is multi-substrate activity and among the twenty amino acids Glutamate, Lysine, Arginine, Serine, Aspartic acid, Glutamine and Thereonine were found to be effective in binding to different type of ligands. -, 09.06.2017, Taschenbuch, Neuware, 220x150x9 mm, 231g, 144, Internationaler Versand, offene Rechnung (Vorkasse vorbehalten), Selbstabholung und Barzahlung, PayPal, Banküberweisung.
3
9783330082946 - Arabinda Ghosh: Insilico analysis of xylanases from thermophilic bacteria
Arabinda Ghosh

Insilico analysis of xylanases from thermophilic bacteria (2017)

Lieferung erfolgt aus/von: Deutschland DE PB NW

ISBN: 9783330082946 bzw. 3330082941, in Deutsch, 144 Seiten, LAP Lambert Academic Publishing, Taschenbuch, neu.

Lieferung aus: Deutschland, Versandkosten nach: Deutschland, Versandkostenfrei.
Von Händler/Antiquariat, Buchhandlung Hoffmann, [3174608].
Neuware - Microorganisms produce enzymes which have the ability convert a given substrate into a desired product. Enzyme became essential components of industries and often called as biocatalyst. Maintaining enzymes and obtaining desired product is a costly affair. In order to overcome such short coming bioinformatics has entered into the field of industrial enzymology. In this study xylanases enzyme from different extremophilic bacteria was selected for which protein were built by homology modeling each of receptors bears partial structural similarity which was also highlighted by similar active site residues but were positioned at different locations. In silico binding affinity of these enzyme shows is multi-substrate activity and among the twenty amino acids Glutamate, Lysine, Arginine, Serine, Aspartic acid, Glutamine and Thereonine were found to be effective in binding to different type of ligands. 09.06.2017, Taschenbuch, Neuware, 220x150x9 mm, 231g, 144, Internationaler Versand, offene Rechnung (Vorkasse vorbehalten), sofortueberweisung.de, Selbstabholung und Barzahlung, Skrill/Moneybookers, PayPal, Lastschrift, Banküberweisung.
4
9783330082946 - Ghosh, Arabinda: Insilico analysis of xylanases from thermophilic bacteria
Symbolbild
Ghosh, Arabinda

Insilico analysis of xylanases from thermophilic bacteria

Lieferung erfolgt aus/von: Deutschland DE PB NW

ISBN: 9783330082946 bzw. 3330082941, in Deutsch, Taschenbuch, neu.

Lieferung aus: Deutschland, Versandkostenfrei.
Von Händler/Antiquariat, European-Media-Service Mannheim [1048135], Mannheim, Germany.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
5
9783330082946 - Arabinda Ghosh: Insilico analysis of xylanases from thermophilic bacteria
Arabinda Ghosh

Insilico analysis of xylanases from thermophilic bacteria (2017)

Lieferung erfolgt aus/von: Deutschland EN PB NW

ISBN: 9783330082946 bzw. 3330082941, in Englisch, 144 Seiten, LAP LAMBERT Academic Publishing, Taschenbuch, neu.

Lieferung aus: Deutschland, Versandfertig in 1 - 2 Werktagen, Versandkostenfrei.
Von Händler/Antiquariat, expressbuch24.
Die Beschreibung dieses Angebotes ist von geringer Qualität oder in einer Fremdsprache. Trotzdem anzeigen
Lade…