1l19

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[[Image:1l19.jpg|left|200px]]
[[Image:1l19.jpg|left|200px]]
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{{Structure
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|PDB= 1l19 |SIZE=350|CAPTION= <scene name='initialview01'>1l19</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1l19", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1l19| PDB=1l19 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l19 OCA], [http://www.ebi.ac.uk/pdbsum/1l19 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l19 RCSB]</span>
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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'''
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Nicholson, H.]]
[[Category: Nicholson, H.]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:25:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:35 2008''
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Revision as of 20:25, 2 May 2008

Image:1l19.jpg

Template:STRUCTURE 1l19

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

1L19 is a Single protein structure of sequence from Enterobacteria phage t4. 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 Page seeded by OCA on Fri May 2 23:25:38 2008

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