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1hj0
From Proteopedia
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| - | [[ | + | ==THYMOSIN BETA9== |
| + | <StructureSection load='1hj0' size='340' side='right' caption='[[1hj0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hj0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HJ0 FirstGlance]. <br> | ||
| + | </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=1hj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hj0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hj0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hj0 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/hj/1hj0_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 == | ||
| + | The conformation of thymosin beta 9 in solution of 40% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol-d2 in water has been investigated by two-dimensional 1H-nmr spectroscopy. Under this condition thymosin beta 9 adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton distance constraints derived from nuclear Overhauser enhancement measurements. The conformation of thymosin beta 9 includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-terminus of thymosin beta 9 shows random-coil structure only. | ||
| - | + | Conformation of thymosin beta 9 in water/fluoroalcohol solution determined by NMR spectroscopy.,Stoll R, Voelter W, Holak TA Biopolymers. 1997 May;41(6):623-34. PMID:9108730<ref>PMID:9108730</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Holak, T A.]] | [[Category: Holak, T A.]] | ||
Revision as of 09:57, 28 September 2014
THYMOSIN BETA9
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