1hj0: Difference between revisions

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New page: left|200px<br /><applet load="1hj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hj0" /> '''THYMOSIN BETA9'''<br /> ==Overview== The co...
 
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[[Image:1hj0.jpg|left|200px]]<br /><applet load="1hj0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hj0.jpg|left|200px]]<br /><applet load="1hj0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hj0" />
caption="1hj0" />
'''THYMOSIN BETA9'''<br />
'''THYMOSIN BETA9'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1HJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HJ0 OCA].  
1HJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJ0 OCA].  


==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Holak, T.A.]]
[[Category: Holak, T A.]]
[[Category: Stoll, R.]]
[[Category: Stoll, R.]]
[[Category: Voelter, W.]]
[[Category: Voelter, W.]]
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[[Category: thymus]]
[[Category: thymus]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:42 2008''

Revision as of 11:01, 21 February 2008

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1hj0

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THYMOSIN BETA9

Overview

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.

About this Structure

1HJ0 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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

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