2f56: Difference between revisions

Revision as of 14:40, 27 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:2f56.png

Template:STRUCTURE 2f56

Barnase cross-linked with glutaraldehyde soaked in 6M ureaBarnase cross-linked with glutaraldehyde soaked in 6M urea

Template:ABSTRACT PUBMED 16600702

About this StructureAbout this Structure

2F56 is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

ReferenceReference

On the edge of the denaturation process: application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations., Salem M, Mauguen Y, Prange T, Biochim Biophys Acta. 2006 May;1764(5):903-12. Epub 2006 Mar 20. PMID:16600702

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+===Barnase cross-linked with glutaraldehyde soaked in 6M urea===
-==Overview==
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-Structural data about the early step of protein denaturation were obtained from cross-linked crystals for two small proteins: barnase and lysozyme. Several denaturant agents like urea, bromoethanol or thiourea were used at increasing concentrations up to a limit leading to crystal disruption (&gt;or=2 to 6 M). Before the complete destruction of the crystal order started, specific binding sites were observed at the protein surfaces, an indication that the preliminary step of denaturation is the disproportion of intermolecular polar bonds to the benefit of the agent "parasiting" the surface. The analysis of the thermal factors first agree with a stabilization effect at low or moderate concentration of denaturants rapidly followed by a destabilization at specific weak points when the number of sites increase (overflooding effect).
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 [[Category: Thiourea]]
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