1hj0: Difference between revisions

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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" />

'''THYMOSIN BETA9'''<br />

==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==

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==

Line 13:

[[Category: Bos taurus]]

[[Category: Single protein]]

[[Category: Holak, T.A.]]

[[Category: Holak, T A.]]

[[Category: Stoll, R.]]

[[Category: Voelter, W.]]

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[[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''

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@@ 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" />
 '''THYMOSIN BETA9'''<br />
 ==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==
-HJ0 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].
+HJ0 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==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Holak, T.A.]]
+[[Category: Holak, T A.]]
 [[Category: Stoll, R.]]
 [[Category: Voelter, W.]]
@@ Line 21: / Line 21: @@
 [[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''