1l20
From Proteopedia
(New page: 200px<br /><applet load="1l20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l20, resolution 1.85Å" /> '''ENHANCED PROTEIN THE...) |
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| - | [[Image:1l20.jpg|left|200px]]<br /><applet load="1l20" size=" | + | [[Image:1l20.jpg|left|200px]]<br /><applet load="1l20" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l20, resolution 1.85Å" /> | caption="1l20, resolution 1.85Å" /> | ||
'''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''<br /> | '''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two different genetically engineered amino-acid substitutions designed to | + | Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix. |
==About this Structure== | ==About this Structure== | ||
| - | 1L20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. 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:// | + | 1L20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. 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=1L20 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Matthews, B | + | [[Category: Matthews, B W.]] |
[[Category: Nicholson, H.]] | [[Category: Nicholson, H.]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:34 2008'' |
Revision as of 11:40, 21 February 2008
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ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Overview
Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.
About this Structure
1L20 is a Single protein structure of sequence from Bacteriophage t4. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317
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