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New page: left|200px<br /><applet load="1z55" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z55, resolution 1.9Å" /> '''Effect of alcohols on...
 
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[[Image:1z55.gif|left|200px]]<br /><applet load="1z55" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1z55, resolution 1.9&Aring;" />
'''Effect of alcohols on protein hydration'''<br />


==Overview==
==Effect of alcohols on protein hydration==
Organic solvents are known to bring about dehydration of proteins, the, molecular basis of which has remained uncharacterized. The dehydration, effect in many cases leads to eventual unfolding of proteins through the, macroscopic solvent effect. In some cases, the organic solvent molecules, also bind to protein surfaces, thereby forcing local unfolding. The X-ray, structure of hen egg-white lysozyme co-crystallized in the presence of, alcohols with varying hydrophobicities has been studied. It was noticed, that although the alcohols have very little effect on the conformation of, the overall protein structure, they profoundly affect protein hydration, and disorder of the bound waters. Systematic analysis of the water, structure around the lysozyme molecule suggests that an increasing order, of hydrophobicity of alcohols is directly proportional to the higher, number of weakly bound waters in the protein. As anticipated, the water, molecules in the native structure with high temperature factors (&gt;/=40, A(2)) attain higher disorder in the presence of alcohols. It is believed, that the disorder induced in the water molecules is a direct consequence, of alcohol binding.
<StructureSection load='1z55' size='340' side='right'caption='[[1z55]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1z55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z55 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z55 OCA], [https://pdbe.org/1z55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z55 RCSB], [https://www.ebi.ac.uk/pdbsum/1z55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z55 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
== 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/z5/1z55_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1z55 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Organic solvents are known to bring about dehydration of proteins, the molecular basis of which has remained uncharacterized. The dehydration effect in many cases leads to eventual unfolding of proteins through the macroscopic solvent effect. In some cases, the organic solvent molecules also bind to protein surfaces, thereby forcing local unfolding. The X-ray structure of hen egg-white lysozyme co-crystallized in the presence of alcohols with varying hydrophobicities has been studied. It was noticed that although the alcohols have very little effect on the conformation of the overall protein structure, they profoundly affect protein hydration and disorder of the bound waters. Systematic analysis of the water structure around the lysozyme molecule suggests that an increasing order of hydrophobicity of alcohols is directly proportional to the higher number of weakly bound waters in the protein. As anticipated, the water molecules in the native structure with high temperature factors (&gt;/=40 A(2)) attain higher disorder in the presence of alcohols. It is believed that the disorder induced in the water molecules is a direct consequence of alcohol binding.


==About this Structure==
Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols.,Deshpande A, Nimsadkar S, Mande SC Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):1005-8. Epub 2005, Jun 24. PMID:15983424<ref>PMID:15983424</ref>
1Z55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z55 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols., Deshpande A, Nimsadkar S, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):1005-8. Epub 2005, Jun 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15983424 15983424]
</div>
<div class="pdbe-citations 1z55" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Deshpande A]]
[[Category: Deshpande, A.]]
[[Category: Mande SC]]
[[Category: Mande, S.C.]]
[[Category: Nimsadkar S]]
[[Category: Nimsadkar, S.]]
[[Category: CL]]
[[Category: NA]]
[[Category: alcohols hydration]]
[[Category: hen egg whit lysozyme]]
[[Category: water structure]]
 
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Latest revision as of 07:44, 30 October 2024

Effect of alcohols on protein hydration

1z55, resolution 1.90Å

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