2l9i: Difference between revisions
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[[ | ==NMR structure of thymosin alpha-1== | ||
<StructureSection load='2l9i' size='340' side='right' caption='[[2l9i]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | |||
== Structural highlights == | |||
[[2l9i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9I OCA]. <br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== 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> | |||
== References == | |||
<references/> | |||
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</StructureSection> | |||
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[[Category: Elizondo-Riojas, M A.]] | [[Category: Elizondo-Riojas, M A.]] | ||
[[Category: Gorenstein, D G.]] | [[Category: Gorenstein, D G.]] | ||