Thesis
Chemical modifications of lysozyme
- Abstract:
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The three-dimensional structure of the glycosidase, hen egg white lysozyme, has been determined by X-ray crystallography; the molecule is roughly ellipsoidal, with a cleft running down one side, and this cleft, which is capable of accommodating up to six sugar residues (in sub-sites A-F) is known to be the site of catalytic action, glycolysis occurring between sites D and E. The only significant enzyme functional groups in this region are the carboxylic acids Asp 52 and Glu 35, and it is ...
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Authors
- Publication date:
- 1970
- DOI:
- Type of award:
- DPhil
- Level of award:
- Doctoral
- Awarding institution:
- University of Oxford
- Language:
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English
- UUID:
-
uuid:454d6c8d-2176-427d-ac38-16e998f051a5
- Local pid:
-
td:601870665
- Source identifiers:
-
601870665
- Deposit date:
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2015-03-26
Terms of use
- Copyright holder:
- Farmer, P. B.
- Copyright date:
- 1970
- Notes:
- This thesis was digitised thanks to the generosity of Dr Leonard Polonsky
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