2mea: Difference between revisions
New page: left|200px<br /> <applet load="2mea" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mea, resolution 2.2Å" /> '''CHANGES IN CONFORMAT... |
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'''CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS'''<br /> | '''CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2MEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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:// | 2MEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2MEA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: o-glycosyl]] | [[Category: o-glycosyl]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:37:55 2008'' | ||
Revision as of 18:37, 15 February 2008
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CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
OverviewOverview
To elucidate correlative relationships between structural change and, thermodynamic stability in proteins, a series of mutant human lysozymes, modified at two buried positions (Ile56 and Ile59) were examined. Their, thermodynamic parameters of denaturation and crystal structures were, studied by calorimetry and X-ray crystallography. The mutants at positions, 56 and 59 exhibited different responses to a series of amino acid, substitutions. The changes in stability due to substitutions showed a, linear correlation with changes in hydrophobicity of substituted residues, having different slopes at each mutation site. However, the stability of, each mutant was found to be represented by a unique equation involving, physical properties calculated from mutant structures. By fitting present, and previous stability data for mutant human lysozymes substituted at, various positions to the equation, the magnitudes of the hydrophobicity of, a carbon atom and the hydrophobicity of nitrogen and neutral oxygen atoms, were found to be 0.178 and -0.013 kJ/mol.A(2), respectively. It was also, found that the contribution of a hydrogen bond with a length of 3.0 A to, protein stability was 5.1 kJ/mol and the entropy loss of newly, introduction of a water molecules was 7.8 kJ/mol.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
2MEA is a Single protein structure of sequence from Homo sapiens. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme., Funahashi J, Takano K, Yamagata Y, Yutani K, Protein Eng. 1999 Oct;12(10):841-50. PMID:10556244
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