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Improving the thermostability of the neutral protease of Bacillus stearothermophilus by replacing a buried asparagine by leucine
Author(s) -
Eijsink Vincent G.H.,
van der Zee Rob,
van den Burg Bertus,
Vriend Gerrit,
Venema Gerard
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80434-5
Subject(s) - thermostability , asparagine , leucine , directed mutagenesis , chemistry , hydrogen bond , amino acid , neutral protease , mutagenesis , protease , side chain , site directed mutagenesis , biochemistry , proline , stereochemistry , mutation , enzyme , organic chemistry , molecule , polymer , mutant , gene
Amino acids buried in the hydrophobic interior of a protein with polar side chain atoms, which are not involved in hydrogen bonding or electrostatic interactions, have an adverse effect on protein stability. Replacing such residues by hydrophobic ones may render a protein more stable. Asparagine 241, which is buried in the neutral protease of Bacillus stearothermophilus , was replaced by leucine by side‐directed mutagenesis. This mutation increased the stability of the protein by 0.7 ± 0.1 degree.