1hj0: Difference between revisions
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==Thymosin beta9== | ==Thymosin beta9== | ||
<StructureSection load='1hj0' size='340' side='right' caption='[[1hj0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1hj0' size='340' side='right'caption='[[1hj0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == 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> | <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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Holak, T A]] | [[Category: Holak, T A]] | ||
[[Category: Stoll, R]] | [[Category: Stoll, R]] | ||
Revision as of 12:54, 30 October 2019
Thymosin beta9Thymosin beta9
Structural highlights
Function[TYB10_BOVIN] Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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