1zw7

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[[Image:1zw7.gif|left|200px]]
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|GENE= UBI1, RPL40A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zw7 OCA], [http://www.ebi.ac.uk/pdbsum/1zw7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zw7 RCSB]</span>
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'''Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences'''
'''Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences'''
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[[Category: Gronenborn, A M.]]
[[Category: Gronenborn, A M.]]
[[Category: Makhatadze, G I.]]
[[Category: Makhatadze, G I.]]
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[[Category: dynamic]]
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[[Category: Dynamic]]
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[[Category: thermodynamic]]
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[[Category: Thermodynamic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:09:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:42:26 2008''
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Revision as of 15:09, 3 May 2008

Template:STRUCTURE 1zw7

Elimination of the C-cap in Ubiquitin Structure, Dynamics and Thermodynamic Consequences


Overview

Single amino acid substitutions rarely produce substantial changes in protein structure. Here we show that substitution of the C-cap residue in the alpha-helix of ubiquitin with proline (34P variant) leads to dramatic structural changes. The resulting conformational perturbation extends over the last two turns of the alpha-helix and leads to enhanced flexibility for residues 27-37. Thermodynamic analysis of this ubiquitin variant using differential scanning calorimetry reveals that the thermal unfolding transition remains highly cooperative, exhibiting two-state behavior. Similarities with the wild type in the thermodynamic parameters (heat capacity change upon unfolding and m-value) of unfolding monitored by DSC and chemical denaturation suggests that the 34P variant has comparable buried surface area. The hydrophobic core of 34P variant is not packed as well as that of the wild type protein as manifested by a lower enthalpy of unfolding. The increased mobility of the polypeptide chain of this ubiquitin variant allows the transient opening of the hydrophobic core as evidenced by ANS binding. Taken together, these results suggest exceptional robustness of cooperativity in protein structures.

About this Structure

1ZW7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Elimination of the C-cap in ubiquitin - structure, dynamics and thermodynamic consequences., Ermolenko DN, Dangi B, Gvritishvili A, Gronenborn AM, Makhatadze GI, Biophys Chem. 2007 Mar;126(1-3):25-35. Epub 2006 Apr 5. PMID:16713063 Page seeded by OCA on Sat May 3 18:09:15 2008

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