Aromatic interactions and rotational strengths within protein environment: An electronic structural study on β-lactamases from class A

Christov, Christo, Karabencheva-Christova, Tatyana and Lodola, Alessio (2008) Aromatic interactions and rotational strengths within protein environment: An electronic structural study on β-lactamases from class A. Chemical Physics Letters, 456 (1-3). pp. 89-95. ISSN 0009-2614

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Official URL: http://dx.doi.org/10.1016/j.cplett.2008.03.012

Abstract

β-Lactamases are important enzymes, responsible for bacterial resistance against β-lactam antibiotics. The enzymes from class A are the most common and the most intensively studied. Here we present our electronic structural study on the relationships between electrostatic interactions and chiroptical properties of three enzymes from class A in the following directions: (i) an integrated influence of environment and ionization state on the rotational strengths mechanisms of tyrosine chromophore in TEM-1 β-lactamase; (ii) an effect of electrostatic environment on the mechanisms of aromatic rotational strengths in β-lactamases from Streptomyces albus and Staphylococcus aureus.

Item Type: Article
Subjects: B400 Nutrition
C100 Biology
Department: Faculties > Health and Life Sciences > School of Life Sciences > Applied Sciences
Related URLs:
Depositing User: Ay Okpokam
Date Deposited: 01 Mar 2012 16:19
Last Modified: 10 Aug 2015 11:46
URI: http://nrl.northumbria.ac.uk/id/eprint/5576

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