1l18
From Proteopedia
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| - | [[ | + | ==HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3== |
| + | <StructureSection load='1l18' size='340' side='right' caption='[[1l18]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1l18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L18 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lzm|2lzm]], [[1l01|1l01]], [[1l02|1l02]], [[1l03|1l03]], [[1l04|1l04]], [[1l05|1l05]], [[1l06|1l06]], [[1l07|1l07]], [[1l08|1l08]], [[1l09|1l09]], [[1l10|1l10]], [[1l11|1l11]], [[1l12|1l12]], [[1l13|1l13]], [[1l14|1l14]], [[1l15|1l15]], [[1l16|1l16]], [[1l17|1l17]], [[1l19|1l19]], [[1l20|1l20]], [[1l21|1l21]], [[1l22|1l22]], [[1l23|1l23]], [[1l24|1l24]], [[1l25|1l25]], [[1l26|1l26]], [[1l27|1l27]], [[1l28|1l28]], [[1l29|1l29]], [[1l30|1l30]], [[1l31|1l31]], [[1l32|1l32]], [[1l33|1l33]], [[1l34|1l34]], [[1l35|1l35]], [[1l36|1l36]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l18 RCSB], [http://www.ebi.ac.uk/pdbsum/1l18 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l18_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Replacing the isoleucine at amino-acid position three of bacteriophage T4 lysozyme causes changes in the thermodynamic stability of the protein that are directly related to the hydrophobicity of the substituted residue. Structural analysis confirms that the hydrophobic stabilization is proportional to the reduction of the surface area accessible to solvent on folding. | ||
| - | + | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.,Matsumura M, Becktel WJ, Matthews BW Nature. 1988 Aug 4;334(6181):406-10. PMID:3405287<ref>PMID:3405287</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Enterobacteria phage t4]] | [[Category: Enterobacteria phage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
Revision as of 18:36, 28 September 2014
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
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