1ios: Difference between revisions
New page: left|200px<br /><applet load="1ios" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ios, resolution 1.76Å" /> '''STABILIZATION OF HEN... |
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[[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size=" | [[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ios, resolution 1.76Å" /> | caption="1ios, resolution 1.76Å" /> | ||
'''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''<br /> | '''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''<br /> | ||
==Overview== | ==Overview== | ||
Stabilization of a protein using cavity-filling strategy has hardly been | 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== | ==About this Structure== | ||
1IOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | 1IOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:01 2008'' | ||
Revision as of 14:14, 21 February 2008
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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
1IOS is a Single protein structure of sequence from Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 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
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