2f4a
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| , resolution 1.95Å | |||||||
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| Ligands: | , , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Related: | 2F2N, 2F30
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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