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'''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION''' | '''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION''' | ||
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[[Category: Saito, M.]] | [[Category: Saito, M.]] | ||
[[Category: Ueda, T.]] | [[Category: Ueda, T.]] | ||
[[Category: | [[Category: Bacteriolytic enzyme]] | ||
[[Category: | [[Category: Glycosidase]] | ||
[[Category: | [[Category: Hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:13:55 2008'' | |||
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Revision as of 20:13, 2 May 2008
STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION
OverviewOverview
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.
About this StructureAbout this Structure
1IOR is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Stabilization of hen egg white lysozyme by a cavity-filling mutation., Ohmura T, Ueda T, Ootsuka K, Saito M, Imoto T, Protein Sci. 2001 Feb;10(2):313-20. PMID:11266617 Page seeded by OCA on Fri May 2 20:13:55 2008