1ios

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{{STRUCTURE_1ios| PDB=1ios | SCENE= }}
{{STRUCTURE_1ios| PDB=1ios | SCENE= }}
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'''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''
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===STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11266617 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11266617}}
==About this Structure==
==About this Structure==
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:14:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:42:59 2008''

Revision as of 10:43, 1 July 2008

Image:1ios.png

Template:STRUCTURE 1ios

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

Template:ABSTRACT PUBMED 11266617

About this Structure

1IOS is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

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

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