1hz1: Difference between revisions

Revision as of 10:09, 1 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:1hz1.png

Template:STRUCTURE 1hz1

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+

Template:ABSTRACT PUBMED 11453993

About this StructureAbout this Structure

1HZ1 is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

ReferenceReference

The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution., Deswarte J, De Vos S, Langhorst U, Steyaert J, Loris R, Eur J Biochem. 2001 Jul;268(14):3993-4000. PMID:11453993

Page seeded by OCA on Tue Jul 1 10:09:23 2008

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OCA

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-'''RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+'''
+===RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+===
-==Overview==
+<!--
-In the crystalline state, ribonuclease T1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution.
+The line below this paragraph, {{ABSTRACT_PUBMED_11453993}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11453993}}
 ==About this Structure==
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 [[Category: Ribonuclease]]
 [[Category: Stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:22:55 2008''
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