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Increased Thermal Stability of Site‐Selectively Glycosylated Dihydrofolate Reductase
Author(s) -
Swanwick Richard S.,
Daines Alison M.,
Tey LaiHock,
Flitsch Sabine L.,
Allemann Rudolf K.
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500103
Subject(s) - dihydrofolate reductase , glycosylation , thermal stability , chemistry , enzyme , biochemistry , organic chemistry
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.