1ioq: Difference between revisions

Revision as of 13:42, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ioq.png

Template:STRUCTURE 1ioq

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

Template:ABSTRACT PUBMED 11266617

About this StructureAbout this Structure

1IOQ 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 Tue Jul 1 13:42:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11266617}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11266617 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11266617}}
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 [[Category: Glycosidase]]
 [[Category: Hydrolase]]
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