Prediction of bond length variation in classical β-lactam structures and enzymatic ring instability-Reference-Cited by-同舟云学术

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Prediction of bond length variation in classical β-lactam structures and enzymatic ring instability

Published:2009-06-19 Issue:S10 Volume:24 Page:231-249
ISSN:0020-7608
Container-title:International Journal of Quantum Chemistry
language:en
Short-container-title:Int. J. Quantum Chem.

Author:

Scanlan M. J.,Hillier I. H.,Hodgkin E. E.,Sidebotham R. P.,Warwick C. M.,Davies R. H.

Publisher

Wiley

Subject

Physical and Theoretical Chemistry,Condensed Matter Physics,Atomic and Molecular Physics, and Optics

Reference56 articles.

1. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

2. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.

3. Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase

4. THEORETICAL STUDIES ON β-LACTAM ANTIBIOTICS:

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