1rbx
From Proteopedia
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| - | [[Image:1rbx.gif|left|200px]] | + | [[Image:1rbx.gif|left|200px]] |
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| - | '''RIBONUCLEASE A (E.C.3.1.27.5) CONTROL''' | + | {{Structure |
| + | |PDB= 1rbx |SIZE=350|CAPTION= <scene name='initialview01'>1rbx</scene>, resolution 1.69Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RIBONUCLEASE A (E.C.3.1.27.5) CONTROL''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RBX is a [ | + | 1RBX is a [[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=1RBX OCA]. |
==Reference== | ==Reference== | ||
| - | The effect of denaturants on protein structure., Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK, Protein Sci. 1997 Aug;6(8):1727-33. PMID:[http:// | + | The effect of denaturants on protein structure., Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK, Protein Sci. 1997 Aug;6(8):1727-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9260285 9260285] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Pancreatic ribonuclease]] | [[Category: Pancreatic ribonuclease]] | ||
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[[Category: rna)]] | [[Category: rna)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:31 2008'' |
Revision as of 11:49, 20 March 2008
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| , resolution 1.69Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RIBONUCLEASE A (E.C.3.1.27.5) CONTROL
Overview
Virtually all studies of the protein-folding reaction add either heat, acid, or a chemical denaturant to an aqueous protein solution in order to perturb the protein structure. When chemical denaturants are used, very high concentrations are usually necessary to observe any change in protein structure. In a solution with such high denaturant concentrations, both the structure of the protein and the structure of the solvent around the protein can be altered. X-ray crystallography is the obvious experimental technique to probe both types of changes. In this paper, we report the crystal structures of dihydrofolate reductase with urea and of ribonuclease A with guanidinium chloride. These two classic denaturants have similar effects on the native structure of the protein. The most important change that occurs is a reduction in the overall thermal factor. These structures offer a molecular explanation for the reduction in mobility. Although the reduction is observed only with the native enzyme in the crystal, a similar decrease in mobility has also been observed in the unfolded state in solution (Makhatadze G, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study.
About this Structure
1RBX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The effect of denaturants on protein structure., Dunbar J, Yennawar HP, Banerjee S, Luo J, Farber GK, Protein Sci. 1997 Aug;6(8):1727-33. PMID:9260285
Page seeded by OCA on Thu Mar 20 13:49:31 2008
