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Keywords:

  • directed evolution;
  • enzyme catalysis;
  • enzymes;
  • protein engineering;
  • protein stability
Thumbnail image of graphical abstract

Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 19 °C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for cosolvent molecules (red dots).