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2lq1

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==Solution structure of de novo designed antifreeze peptide 3==
==Solution structure of de novo designed antifreeze peptide 3==
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<StructureSection load='2lq1' size='340' side='right'caption='[[2lq1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lq1' size='340' side='right'caption='[[2lq1]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lq1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lq1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glaciozyma_antarctica Glaciozyma antarctica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQ1 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lq0|2lq0]], [[2lq2|2lq2]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq1 OCA], [https://pdbe.org/2lq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq1 ProSAT]</span></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=2lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lq1 OCA], [https://pdbe.org/2lq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2lq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lq1 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D0EKL2_9BASI D0EKL2_9BASI]
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Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several alpha-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of alpha-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
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Solution structures, dynamics, and ice growth inhibitory activity of Peptide fragments derived from an antarctic yeast protein.,Shah SH, Kar RK, Asmawi AA, Rahman MB, Murad AM, Mahadi NM, Basri M, Rahman RN, Salleh AB, Chatterjee S, Tejo BA, Bhunia A PLoS One. 2012;7(11):e49788. doi: 10.1371/journal.pone.0049788. Epub 2012 Nov 28. PMID:23209600<ref>PMID:23209600</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 2lq1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glaciozyma antarctica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhunia, A]]
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[[Category: Bhunia A]]
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[[Category: Afp]]
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[[Category: Antifreeze protein]]
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Current revision

Solution structure of de novo designed antifreeze peptide 3

PDB ID 2lq1

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