1dds

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dds.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dds.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dds| PDB=1dds | SCENE= }}
{{STRUCTURE_1dds| PDB=1dds | SCENE= }}
-
'''MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE'''
+
===MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9260285}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9260285 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9260285}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Yennawar, H P.]]
[[Category: Yennawar, H P.]]
[[Category: Oxido-reductase]]
[[Category: Oxido-reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:44:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:52:32 2008''

Revision as of 19:52, 30 June 2008

Image:1dds.png

Template:STRUCTURE 1dds

MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE

Template:ABSTRACT PUBMED 9260285

About this Structure

1DDS is a Single protein structure of sequence from Escherichia coli. 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 Mon Jun 30 22:52:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dds"
Personal tools