Removal of surface charge‐charge interactions from ubiquitin leaves the protein folded and very stable
- 1 January 2002
- journal article
- Published by Wiley in Protein Science
- Vol. 11 (1), 174-177
- https://doi.org/10.1110/ps.29902
Abstract
The contribution of solvent-exposed charged residues to protein stability was evaluated using ubiquitin as a model protein. We combined site-directed mutagenesis and specific chemical modifications to first replace all Arg residues with Lys, followed by carbomylation of Lys-amino groups. Under the conditions in which all carboxylic groups are protonated (at pH 2), the chemically modified protein is folded and very stable (DeltaG = 18 kJ/mol). These results indicate that surface charge-charge interactions are not an essential fundamental force for protein folding and stability.Keywords
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