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Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable

Department of Biochemistry and Molecular Biology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, USA

Reprint requests to: George I. Makhatadze, Department of Biochemistry and Molecular Biology, Penn State University College of Medicine, Hershey, PA 17033; e-mail: makhatadze{at}psu.edu; fax: (717) 531-7072.

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 (G = 18 kJ/mol). These results indicate that surface charge–charge interactions are not an essential fundamental force for protein folding and stability.

Keywords: Protein stability; chemical denaturation; chemical modification; energetics; electrostatic interactions; circular dichroism spectroscopy; balance of forces

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