2f4a

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[[Image:2f4a.gif|left|200px]]
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{{STRUCTURE_2f4a| PDB=2f4a | SCENE= }}
{{STRUCTURE_2f4a| PDB=2f4a | SCENE= }}
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'''Triclinic cross-linked lysozyme soaked with thiourea 1.5M'''
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===Triclinic cross-linked lysozyme soaked with thiourea 1.5M===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 16600702 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16600702}}
==About this Structure==
==About this Structure==
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[[Category: Thiourea]]
[[Category: Thiourea]]
[[Category: Urea]]
[[Category: Urea]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:45:30 2008''

Revision as of 19:45, 28 July 2008

Template:STRUCTURE 2f4a

Triclinic cross-linked lysozyme soaked with thiourea 1.5M

Template:ABSTRACT PUBMED 16600702

About this Structure

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