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Mutation of exposed hydrophobic amino acids to arginine to increase protein stability.

Authors
  • Strub, Caroline
  • Alies, Carole
  • Lougarre, Andrée
  • Ladurantie, Caroline
  • Czaplicki, Jerzy
  • Fournier, Didier
Type
Published Article
Journal
BMC Biochemistry
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Jul 13, 2004
Volume
5
Pages
9–9
Identifiers
PMID: 15251041
Source
Medline
License
Unknown

Abstract

Although 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.

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