2f4a: Difference between revisions

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[[Image:2f4a.gif|left|200px]]<br /><applet load="2f4a" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2f4a.gif|left|200px]]
caption="2f4a, resolution 1.95&Aring;" />
 
'''Triclinic cross-linked lysozyme soaked with thiourea 1.5M'''<br />
{{Structure
|PDB= 2f4a |SIZE=350|CAPTION= <scene name='initialview01'>2f4a</scene>, resolution 1.95&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=TOU:THIOUREA'>TOU</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''Triclinic cross-linked lysozyme soaked with thiourea 1.5M'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2F4A 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>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=TOU:'>TOU</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=2F4A OCA].  
2F4A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F4A OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16600702 16600702]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16600702 16600702]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: barnase]]
[[Category: barnase]]
[[Category: bromoethanol]]
[[Category: bromoethanol]]
[[Category: cross-linked crystals]]
[[Category: cross-linked crystal]]
[[Category: denaturation]]
[[Category: denaturation]]
[[Category: glutaraldehyde]]
[[Category: glutaraldehyde]]
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[[Category: urea]]
[[Category: urea]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:34 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:47:54 2008''

Revision as of 17:47, 20 March 2008

File:2f4a.gif


PDB ID 2f4a

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , and
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



Triclinic cross-linked lysozyme soaked with thiourea 1.5M


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

2F4A is a Single protein structure of sequence from Gallus gallus. 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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