Nisin Based Lantibiotic Engineering: A Novel Approach On Biopreservation. Cet article n’est pas disponible.
Mohanasrinivasan, V.; Devi, C.Subathra; E., Suganthi V. Selvarajan; Mohanasrinivasan, V.; Devi, C.Subathra; E., Suganthi V. Selvarajan
Langue : anglais
Edité par Lap Lambert Academic Publishing, 2012
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- Neuf

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A propos de cet article
80 pages. 8.66x5.91x0.19 inches. In Stock.
N° de réf. du vendeur 3659254738
- Titre
- Nisin Based Lantibiotic Engineering: A Novel Approach On Biopreservation
- Auteur
- Mohanasrinivasan, V.; Devi, C.Subathra; E., Suganthi V. Selvarajan; Mohanasrinivasan, V.; Devi, C.Subathra; E., Suganthi V. Selvarajan
- Éditeur
- Lap Lambert Academic Publishing
- Année de publication
- 2012
- État de l'article
- Brand New
- Reliure
- Paperback
- Langue
- anglais
- ISBN à 10 chiffres
- 3659254738
- ISBN à 13 chiffres
- 9783659254734
- Poids de l'article
- 0,17 kilogramme
Lantibiotics are ribosomally synthesized polycyclic peptide containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and there by lyses the cell. Nisin is the one of the most studied commonly used lantibiotics. Nisin inhibit the growth of bacteria by inhibiting cell wall synthesis via binding to Lipid II. Nisin have thio esters five ring system. But first three are actively involved in antimicrobial activity. These are binding to pyrophosphate moiety of lipid II. This mode of action is the rationale for design of small nisin derived peptide to obtain novel potential lantibiotics. As conformational constraints the Thioether Bridge was mimicked by alkanes or alkenes by ring closing metathesis.
« Synopsis » peut appartenir à une autre édition de cet ouvrage.
Présentation de l'éditeur
Lantibiotics are ribosomally synthesized polycyclic peptide containing unusual amino acids, which have binding specificity for bacterial cells, targeting the bacterial cell wall component lipid II to form pores and there by lyses the cell. Nisin is the one of the most studied commonly used lantibiotics. Nisin inhibit the growth of bacteria by inhibiting cell wall synthesis via binding to Lipid II. Nisin have thio esters five ring system. But first three are actively involved in antimicrobial activity. These are binding to pyrophosphate moiety of lipid II. This mode of action is the rationale for design of small nisin derived peptide to obtain novel potential lantibiotics. As conformational constraints the Thioether Bridge was mimicked by alkanes or alkenes by ring closing metathesis.
« A propos de ce titre » peut appartenir à une autre édition de cet ouvrage.