Mutation of exposed hydrophobic amino acids to arginine to increase protein stabilityReport as inadecuate

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BMC Biochemistry

, 5:9

First Online: 13 July 2004Received: 25 February 2004Accepted: 13 July 2004


BackgroundOne strategy to increase the stability of proteins is to reduce the area of water-accessible hydrophobic surface.

ResultsIn order to test it, we replaced 14 solvent-exposed hydrophobic residues of acetylcholinesterase by arginine. The stabilities of the resulting proteins were tested using denaturation by high temperature, organic solvents, urea and by proteolytic digestion.

ConclusionAltough the mutational effects were rather small, this strategy proved to be successful since half of the mutants showed an increased stability. This stability may originate from the suppression of unfavorable interactions of nonpolar residues with water or from addition of new hydrogen bonds with the solvent. Other mechanisms may also contribute to the increased stability observed with some mutants. For example, introduction of a charge at the surface of the protein may provide a new coulombic interaction on the protein surface.

List of abbreviationsAChEacetylcholinesterase

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2091-5-9 contains supplementary material, which is available to authorized users.

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Author: Caroline Strub - Carole Alies - Andrée Lougarre - Caroline Ladurantie - Jerzy Czaplicki - Didier Fournier


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