Stabilization of hen egg white lysozyme by a cavity-filling mutation

Tadahiro Ohmura, Tadashi Ueda, Keiichi Ootsuka, Minoru Saito, Taiji Imoto

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)


Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully.

Original languageEnglish
Pages (from-to)313-320
Number of pages8
JournalProtein Science
Issue number2
Publication statusPublished - 2001

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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