2op2: Difference between revisions

Revision as of 05:07, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2op2.png

Template:STRUCTURE 2op2

Crystal structure of RNase double-mutant V43C R85C with extra disulphide bondCrystal structure of RNase double-mutant V43C R85C with extra disulphide bond

Template:ABSTRACT PUBMED 17937908

About this StructureAbout this Structure

2OP2 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Implementation of a k/k(0) method to identify long-range structure in transition states during conformational folding/unfolding of proteins., Pradeep L, Kurinov I, Ealick SE, Scheraga HA, Structure. 2007 Oct;15(10):1178-89. PMID:17937908

Page seeded by OCA on Tue Jul 29 05:07:10 2008

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

OCA

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-'''Crystal structure of RNase double-mutant V43C R85C with extra disulphide bond'''
+===Crystal structure of RNase double-mutant V43C R85C with extra disulphide bond===
-==Overview==
+<!--
-A previously introduced kinetic-rate constant (k/k(0)) method, where k and k(0) are the folding (unfolding) rate constants in the mutant and the wild-type forms, respectively, of a protein, has been applied to obtain qualitative information about structure in the transition state ensemble (TSE) of bovine pancreatic ribonuclease A (RNase A), which contains four native disulfide bonds. The method compares the folding (unfolding) kinetics of RNase A, with and without a covalent crosslink and tests whether the crosslinked residues are associated in the folding (unfolding) transition state (TS) of the noncrosslinked version. To confirm that the fifth disulfide bond has not introduced a significant structural perturbation, we solved the crystal structure of the V43C-R85C mutant to 1.6 A resolution. Our findings suggest that residues Val43 and Arg85 are not associated, and that residues Ala4 and Val118 may form nonnative contacts, in the folding (unfolding) TSE of RNase A.
+The line below this paragraph, {{ABSTRACT_PUBMED_17937908}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17937908 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17937908}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Rnase]]
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