1iot
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(New page: 200px<br /><applet load="1iot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iot, resolution 1.75Å" /> '''STABILIZATION OF HEN...)
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Revision as of 15:26, 20 November 2007
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STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION
Overview
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 Structure
1IOT 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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