2f5m

From Proteopedia

Revision as of 08:15, 21 November 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

2f5m, resolution 1.95Å

Drag the structure with the mouse to rotate

Cross-linked barnase soaked in bromo-ethanol

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

2F5M is a Single protein structure of sequence from Bacillus amyloliquefaciens with BRJ as ligand. 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

Page seeded by OCA on Wed Nov 21 10:22:47 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools