Increased Thermal Stability of Site-Selectively Glycosylated Dihydrofolate Reductase

Swanwick, Richard S., Daines, Alison M., Tey, Lai-Hock, Flitsch, Sabine L. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2005. Increased Thermal Stability of Site-Selectively Glycosylated Dihydrofolate Reductase. ChemBioChem 6 (8) , pp. 1338-1340. 10.1002/cbic.200500103

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Abstract

Heat protection. The native conformation of many proteins can be stabilised against thermal denaturation by glycosylation. Here we show that the thermal stability of the naturally nonglycosylated enzyme, dihydrofolate reductase, can be increased significantly by site-selective glycosylation (see figure). The data suggest that increases in thermal stability can be achieved even with the small carbohydrates used in this study.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Uncontrolled Keywords:	glycosylation; mutagenesis; oligosaccharides; selectivity; thermal stability
Publisher:	Wiley-Blackwell
ISSN:	1439-4227
Last Modified:	18 Oct 2022 13:19
URI:	https://orca.cardiff.ac.uk/id/eprint/13489

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