1l19: Difference between revisions
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==ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES== | ==ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES== | ||
<StructureSection load='1l19' size='340' side='right' caption='[[1l19]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1l19' size='340' side='right'caption='[[1l19]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l19]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L19 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1l19]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L19 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l19_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l19_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bpt4]] | [[Category: Bpt4]] | ||
[[Category: Large Structures]] | |||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Matthews, B W]] | [[Category: Matthews, B W]] | ||
[[Category: Nicholson, H]] | [[Category: Nicholson, H]] | ||
Revision as of 15:26, 13 November 2019
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLESENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Structural highlights
Function[LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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