This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hj0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1hj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hj0" /> '''THYMOSIN BETA9'''<br /> ==Overview== The co...)
Line 1: Line 1:
-
[[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==
Line 13: Line 13:
[[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.]]
Line 21: Line 21:
[[Category: thymus]]
[[Category: thymus]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:36:18 2007''
+
''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


1hj0

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:01:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools