2f56

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(New page: 200px<br /><applet load="2f56" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f56, resolution 1.955&Aring;" /> '''Barnase cross-linke...)
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[[Image:2f56.gif|left|200px]]<br /><applet load="2f56" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2f56, resolution 1.955&Aring;" />
caption="2f56, resolution 1.955&Aring;" />
'''Barnase cross-linked with glutaraldehyde soaked in 6M urea'''<br />
'''Barnase cross-linked with glutaraldehyde soaked in 6M urea'''<br />
==Overview==
==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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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).
==About this Structure==
==About this Structure==
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2F56 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with ZN and URE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F56 OCA].
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2F56 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=URE:'>URE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F56 OCA].
==Reference==
==Reference==
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[[Category: urea]]
[[Category: urea]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:22:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:48 2008''

Revision as of 15:17, 21 February 2008

Image:2f56.gif

2f56, resolution 1.955Å

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Barnase cross-linked with glutaraldehyde soaked in 6M urea

Overview

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 (>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).

About this Structure

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

Reference

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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