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Stabilization of hen egg white lysozyme by a cavity‐filling mutation
Author(s) -
Ohmura Tadahiro,
Ueda Tadashi,
Ootsuka Keiichi,
Saito Minoru,
Imoto Taiji
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.37401
Subject(s) - lysozyme , van der waals force , mutation , egg white , chemistry , mutant , crystallography , biophysics , biology , biochemistry , molecule , organic chemistry , gene
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.