Use this URL to cite or link to this record in EThOS: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.687436 |
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Title: | Modelling catalysis in hen egg-white lysozyme | ||||
Author: | Limb, Michael |
ISNI:
0000 0004 5923 7088
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Awarding Body: | University of Bristol | ||||
Current Institution: | University of Bristol | ||||
Date of Award: | 2015 | ||||
Availability of Full Text: |
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Abstract: | |||||
Hen egg-white lysozyme (HEWL), a paradigmatic glycoside hydrolase (GH), is a retaining
β-glycosidase catalysing the cleavage of β-glycosidic bonds found in the cell wall of Grampositive bacteria. Despite extensive research, the nature and role of substrate distortion in catalysis is still unclear. Here, MM and QM/MM modelling was performed on a HEWL trisaccharide (NAM-B-β(1→4)-NAG-C-β(1→4)-NAM-D) product complex to investigate distortion and reactivity of the NAM-D ring bound in the -1 site of the enzyme.
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Supervisor: | Not available | Sponsor: | Not available | ||
Qualification Name: | Thesis (Ph.D.) | Qualification Level: | Doctoral | ||
EThOS ID: | uk.bl.ethos.687436 | DOI: | Not available | ||
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