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Protein stabilisation by compatible solutes: effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A.

Abstract:

Differential scanning calorimetry, optical spectroscopy, and activity measurements were used to investigate the effect of mannosylglycerate, a negatively charged osmolyte widely distributed among thermophilic and hyperthermophilic archaea and bacteria, on the thermal unfolding of ribonuclease A (RNase A). For comparison, assays in the presence of trehalose, a canonical solute in mesophiles, and potassium chloride were also carried out. A thermodynamic analysis was performed by using different...

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Publisher copy:
10.1002/cbic.200300574

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Journal:
Chembiochem : a European journal of chemical biology
Volume:
4
Issue:
8
Pages:
734-741
Publication date:
2003-08-01
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
Source identifiers:
416745
Language:
English
Keywords:
Pubs id:
pubs:416745
UUID:
uuid:03029678-0c57-48f0-acd7-122dfc53780b
Local pid:
pubs:416745
Deposit date:
2013-11-17

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