1gf7
From Proteopedia
(New page: 200px<br /> <applet load="1gf7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gf7, resolution 1.8Å" /> '''BURIED POLAR MUTANT ...) |
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caption="1gf7, resolution 1.8Å" /> | caption="1gf7, resolution 1.8Å" /> | ||
'''BURIED POLAR MUTANT HUMAN LYSOZYME'''<br /> | '''BURIED POLAR MUTANT HUMAN LYSOZYME'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GF7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1GF7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1GF7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: stability]] | [[Category: stability]] | ||
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Revision as of 13:53, 15 February 2008
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BURIED POLAR MUTANT HUMAN LYSOZYME
Contents |
Overview
It has been generally believed that polar residues are usually located on, the surface of protein structures. However, there are many polar groups in, the interior of the structures in reality. To evaluate the contribution of, such buried polar groups to the conformational stability of a protein, nonpolar to polar mutations (L8T, A9S, A32S, I56T, I59T, I59S, A92S, V93T, A96S, V99T, and V100T) in the interior of a human lysozyme were examined., The thermodynamic parameters for denaturation were determined using a, differential scanning calorimeter, and the crystal structures were, analyzed by X-ray crystallography. If a polar group had a heavy energy, cost to be buried, a mutant protein would be remarkably destabilized., However, the stability (Delta G) of the Ala to Ser and Val to Thr mutant, human lysozymes was comparable to that of the wild-type protein, suggesting a low-energy penalty of buried polar groups. The structural, analysis showed that all polar side chains introduced in the mutant, proteins were able to find their hydrogen bond partners, which are, ubiquitous in protein structures. The empirical structure-based, calculation of stability change (Delta Delta G) [Takano et al. (1999), Biochemistry 38, 12698--12708] revealed that the mutant proteins decreased, the hydrophobic effect contributing to the stability (Delta G(HP)), but, this destabilization was recovered by the hydrogen bonds newly introduced., The present study shows the favorable contribution of polar groups with, hydrogen bonds in the interior of protein molecules to the conformational, stability.
Disease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this Structure
1GF7 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Contribution of polar groups in the interior of a protein to the conformational stability., Takano K, Yamagata Y, Yutani K, Biochemistry. 2001 Apr 17;40(15):4853-8. PMID:11294653
Page seeded by OCA on Fri Feb 15 15:53:09 2008
Categories: Homo sapiens | Lysozyme | Single protein | Takano, K. | Yamagata, Y. | Yutani, K. | NA | Buried polar | Stability
