2l9i: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==NMR structure of thymosin alpha-1== | ||
<StructureSection load='2l9i' size='340' side='right'caption='[[2l9i]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2l9i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9I FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 21 models</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=2l9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9i OCA], [https://pdbe.org/2l9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9i RCSB], [https://www.ebi.ac.uk/pdbsum/2l9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
800MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double beta-turns in the N-terminal twelve residues which form a distorted helical structure. | |||
NMR structure of human thymosin alpha-1.,Elizondo-Riojas MA, Chamow SM, Tuthill CW, Gorenstein DG, Volk DE Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):356-61. Epub 2011 Nov 15. PMID:22115779<ref>PMID:22115779</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2l9i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | |||
[[Category: Elizondo-Riojas MA]] | |||
== | [[Category: Gorenstein DG]] | ||
< | [[Category: Volk DE]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||