1ios: Difference between revisions

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[[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ios, resolution 1.76Å" />

'''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''<br />

==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.

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==

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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA].

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==

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[[Category: hydrolase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:33:~~12 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ios.gif|left|200px]]<br /><applet load="1ios" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ios, resolution 1.76&Aring;" />
 '''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''<br />
 ==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.
+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==
-IOS 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA].
+IOS 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==
@@ Line 23: / Line 23: @@
 [[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:33:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:01 2008''