1cjq: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cjq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cjq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJQ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjq RCSB], [http://www.ebi.ac.uk/pdbsum/1cjq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjq RCSB], [http://www.ebi.ac.uk/pdbsum/1cjq PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease|Ribonuclease]] | ||
*[[Temp|Temp]] | |||
*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Ratnaparkhi, G S | [[Category: Ratnaparkhi, G S]] | ||
[[Category: Varadarajan, R | [[Category: Varadarajan, R]] | ||
[[Category: Denaturation]] | [[Category: Denaturation]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Ribonuclease]] | [[Category: Ribonuclease]] | ||
Revision as of 02:44, 23 December 2014
X-RAY CRYSTALLOGRAPHIC STUDIES OF THE DENATURATION OF THE DENATURATION OF RIBONUCLEASE S.X-RAY CRYSTALLOGRAPHIC STUDIES OF THE DENATURATION OF THE DENATURATION OF RIBONUCLEASE S.
Structural highlights
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 PubMedIn 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. X-ray crystallographic studies of the denaturation of ribonuclease S.,Ratnaparkhi GS, Varadarajan R Proteins. 1999 Aug 15;36(3):282-94. PMID:10409822[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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