1cjq: Difference between revisions

Revision as of 13:06, 21 February 2008

X-RAY CRYSTALLOGRAPHIC STUDIES OF THE DENATURATION OF THE DENATURATION OF RIBONUCLEASE S.

OverviewOverview

In an attempt to view the onset of urea denaturation in ribonuclease we have collected X-ray diffraction data on ribonuclease S crystals soaked in 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals were stabilized by glutaraldehyde crosslinking. We have also collected data on ribonuclease S crystals at low pH in an attempt to study the onset of pH denaturation. The resolution of the datasets range from 1.9 to 3.0 A. Analysis of the structures reveals an increase in disorder with increasing urea concentration. In the 5 M urea structure, this increase in disorder is apparent all over the structure but is larger in loop and helical regions than in the beta strands. The low pH structure shows a very similar pattern of increased disorder. In addition there is a major change in the position of the main chain (> 1 A) in the 65-72 turn region. This region has previously been shown to be involved in one of the initial steps of unfolding in the reduction of ribonuclease A. Crystallographic analyses in the presence of denaturant, when combined with controlled crosslinking, can thus provide detailed structural information that is related to the initial steps of unfolding in solution. Proteins 1999;36:282-294.

About this StructureAbout this Structure

1CJQ is a Protein complex structure of sequences from Bos taurus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

X-ray crystallographic studies of the denaturation of ribonuclease S., Ratnaparkhi GS, Varadarajan R, Proteins. 1999 Aug 15;36(3):282-94. PMID:10409822

Page seeded by OCA on Thu Feb 21 12:06:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1cjq.gif|left|200px]]<br /><applet load="1cjq" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cjq.gif|left|200px]]<br /><applet load="1cjq" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cjq, resolution 3.00&Aring;" />
 '''X-RAY CRYSTALLOGRAPHIC STUDIES OF THE DENATURATION OF THE DENATURATION OF RIBONUCLEASE S.'''<br />
 ==Overview==
-In an attempt to view the onset of urea denaturation in ribonuclease we, have collected X-ray diffraction data on ribonuclease S crystals soaked in, 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals, were stabilized by glutaraldehyde crosslinking. We have also collected, data on ribonuclease S crystals at low pH in an attempt to study the onset, of pH denaturation. The resolution of the datasets range from 1.9 to 3.0, A. Analysis of the structures reveals an increase in disorder with, increasing urea concentration. In the 5 M urea structure, this increase in, disorder is apparent all over the structure but is larger in loop and, helical regions than in the beta strands. The low pH structure shows a, very similar pattern of increased disorder. In addition there is a major, change in the position of the main chain (&gt; 1 A) in the 65-72 turn region., This region has previously been shown to be involved in one of the initial, steps of unfolding in the reduction of ribonuclease A. Crystallographic, analyses in the presence of denaturant, when combined with controlled, crosslinking, can thus provide detailed structural information that is, related to the initial steps of unfolding in solution. Proteins, 1999;36:282-294.
+In an attempt to view the onset of urea denaturation in ribonuclease we have collected X-ray diffraction data on ribonuclease S crystals soaked in 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals were stabilized by glutaraldehyde crosslinking. We have also collected data on ribonuclease S crystals at low pH in an attempt to study the onset of pH denaturation. The resolution of the datasets range from 1.9 to 3.0 A. Analysis of the structures reveals an increase in disorder with increasing urea concentration. In the 5 M urea structure, this increase in disorder is apparent all over the structure but is larger in loop and helical regions than in the beta strands. The low pH structure shows a very similar pattern of increased disorder. In addition there is a major change in the position of the main chain (&gt; 1 A) in the 65-72 turn region. This region has previously been shown to be involved in one of the initial steps of unfolding in the reduction of ribonuclease A. Crystallographic analyses in the presence of denaturant, when combined with controlled crosslinking, can thus provide detailed structural information that is related to the initial steps of unfolding in solution. Proteins 1999;36:282-294.
 ==About this Structure==
-CJQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJQ OCA].
+CJQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJQ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Protein complex]]
-[[Category: Ratnaparkhi, G.S.]]
+[[Category: Ratnaparkhi, G S.]]
 [[Category: Varadarajan, R.]]
 [[Category: SO4]]
@@ Line 19: / Line 19: @@
 [[Category: ribonuclease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:31:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:46 2008''