4i5z

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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bn1|2bn1]], [[4i5y|4i5y]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bn1|2bn1]], [[4i5y|4i5y]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">INS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5z RCSB], [http://www.ebi.ac.uk/pdbsum/4i5z PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5z OCA], [http://pdbe.org/4i5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i5z RCSB], [http://www.ebi.ac.uk/pdbsum/4i5z PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN]] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
[[http://www.uniprot.org/uniprot/INS_BOVIN INS_BOVIN]] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Crystallization is a highly demanding and time-consuming task that causes a real bottle-neck in basic research. Great effort has been made to understand the factors and parameters that influence this process and to finely tune them to facilitate crystal growth. Different crystallization techniques have been proposed over the past decades, such as the classical vapor hanging drop method, its variant the sitting drop method, dialysis, cryo-temperature, gel, batch, and the innovative microgravity (space) techniques like free interface diffusion (FID) and counter-ion diffusion (CID). Here, we present a review of the strategies utilizing Langmuir-Blodgett (LB)-based nanotechnologies, and microgravity techniques for obtaining optimal high-quality crystals, as proven by molecular dynamics (MD) and bioinformatics approaches, namely using a clustering algorithm and protein alignment.
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A review of the strategies for obtaining high-quality crystals utilizing nanotechnologies and microgravity.,Pechkova E, Bragazzi N, Bozdaganyan M, Belmonte L, Nicolini C Crit Rev Eukaryot Gene Expr. 2014;24(4):325-39. PMID:25403962<ref>PMID:25403962</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4i5z" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Molecular Playground/Insulin|Molecular Playground/Insulin]]
*[[Molecular Playground/Insulin|Molecular Playground/Insulin]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 07:14, 9 December 2015

Insulin protein crystallization via langmuir-blodgett

4i5z, resolution 1.80Å

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