1hyf

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{{STRUCTURE_1hyf| PDB=1hyf | SCENE= }}
{{STRUCTURE_1hyf| PDB=1hyf | SCENE= }}
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'''RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+'''
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===RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11453993 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11453993}}
==About this Structure==
==About this Structure==
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[[Category: Ribonuclease]]
[[Category: Ribonuclease]]
[[Category: Stability]]
[[Category: Stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:21:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:07:37 2008''

Revision as of 07:07, 1 July 2008

Image:1hyf.png

Template:STRUCTURE 1hyf

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+

Template:ABSTRACT PUBMED 11453993

About this Structure

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

Reference

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

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