2f30: Difference between revisions

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New page: left|200px<br /><applet load="2f30" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f30, resolution 1.65Å" /> '''Triclinic cross-link...
 
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[[Image:2f30.gif|left|200px]]<br /><applet load="2f30" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2f30.gif|left|200px]]<br /><applet load="2f30" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2f30, resolution 1.65&Aring;" />
caption="2f30, resolution 1.65&Aring;" />
'''Triclinic cross-linked Lysozyme soaked with 4.5M urea'''<br />
'''Triclinic cross-linked Lysozyme soaked with 4.5M urea'''<br />


==Overview==
==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, (&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).
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==
2F30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NO3 and URE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F30 OCA].  
2F30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=URE:'>URE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F30 OCA].  


==Reference==
==Reference==
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[[Category: urea]]
[[Category: urea]]


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Revision as of 18:17, 21 February 2008

File:2f30.gif


2f30, resolution 1.65Å

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Triclinic cross-linked Lysozyme soaked with 4.5M urea

OverviewOverview

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 StructureAbout this Structure

2F30 is a Single protein structure of sequence from Gallus gallus with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 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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