| dc.contributor.advisor | Rao, V S R | |
| dc.contributor.author | Virudachalam, R | |
| dc.date.accessioned | 2026-03-10T10:27:23Z | |
| dc.date.available | 2026-03-10T10:27:23Z | |
| dc.date.submitted | 1978 | |
| dc.identifier.uri | https://etd.iisc.ac.in/handle/2005/8999 | |
| dc.description.abstract | Penicillins and cephalosporins are conformationally similar to D-L-Ala-D-Ala due to the presence of the lactam ring.
The mode of binding of the aminoacyl group of penicillin and cephalosporin with transpeptidase is the same, while that of the carboxyl group seems to be different.
The C6 or C7 epimers of penicillins and cephalosporins are completely inactive, since they cannot assume the required conformation to bind with transpeptidase. The 6? or 7? derivatives and the ?-sulfoxide derivative are less active because of the influence of these groups on the required conformation of the aminoacyl group.
To bind with the enzyme, the substrate X-D-Ala-D-Ala should assume conformations around ? ~ 180°, ? ~ -125°, ? ~ 160° and ? ~ 5°. Compared to penicillin, the above conformation is energetically less favoured for the substrate, and this explains the competitive inhibitory property of the antibiotic. | |
| dc.language.iso | en_US | |
| dc.relation.ispartofseries | T01465 | |
| dc.rights | I grant Indian Institute of Science the right to archive and to make available my thesis or dissertation in whole or in part in all forms of media, now hereafter known. I retain all proprietary rights, such as patent rights. I also retain the right to use in future works (such as articles or books) all or part of this thesis or dissertation | |
| dc.subject | Steric maps | |
| dc.subject | Potential energy | |
| dc.subject | Conformation | |
| dc.title | Conformation of peptidoglycan and mode of penicillin action | |
| dc.type | Thesis | |
| dc.degree.name | PhD | |
| dc.degree.level | Doctoral | |
| dc.degree.grantor | Indian Institute of Science | |
| dc.degree.discipline | Science | |
