title: Mutation of exposed hydrophobic amino acids to arginine to increase protein stability.
abstract: BACKGROUND
  One strategy to increase the stability of proteins is to reduce the area of water-accessible hydrophobic surface.
  
  
  RESULTS
  In 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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Institut de Pharmacologie et de Biologie Structurale, 31077 Toulouse, France. caroline_strub@hotmail.com
authors.forename: Caroline
authors.initials: C
authors.lastname: Strub
authors.forename: Carole
authors.initials: C
authors.lastname: Alies
authors.forename: Andrée
authors.initials: A
authors.lastname: Lougarre
authors.forename: Caroline
authors.initials: C
authors.lastname: Ladurantie
authors.forename: Jerzy
authors.initials: J
authors.lastname: Czaplicki
authors.forename: Didier
authors.initials: D
authors.lastname: Fournier
mesh_terms: D000110:Acetylcholinesterase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D000596:Amino Acids / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D001120:Arginine / Q000737:chemistry*; D029721:Drosophila Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D004795:Enzyme Stability / Q000235:genetics; D009154:Mutation / Q000235:genetics*
chemical_list: D000596:Amino Acids; D029721:Drosophila Proteins; D001120:Arginine; D000110:Acetylcholinesterase