Refolding of a high molecular weight protein: salt effect on collapse

Biophysical Journal
D LairezJ Pelta

Abstract

Small-angle neutron scattering experiments were performed on dilute solutions of a high molecular weight protein (fibronectin, M = 580 kg/mol) in four cases: native conditions; unfolded state obtained by a denaturing agent (urea); and two badly refolded (or collapsed) states obtained by progressive elimination of the denaturing agent in salt-containing or salt-free solutions. Our main result is concerned by the conformation of the protein as the attempt for refolding is driven with or without salt. In salt-containing solution, we observe unambiguously that the protein chain collapses at large length scales but still obeys to a Gaussian statistics at short length scales. In other words, the globule embodies a large quantity of solvent compared to the compact situation. In salt-free solutions, the badly refolded protein is not globular but displays both a coil-like and an open conformation at large length scales and a local high density area. This behavior is discussed with respect to the scaling theories for polymers and polyampholytes.

References

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Citations

Aug 13, 2011·Journal of Fluorescence·Afshin Iram, Aabgeena Naeem
May 16, 2006·The International Journal of Biochemistry & Cell Biology·Salima PatelEmmanuel Pauthe
Aug 7, 2007·Physical Review Letters·D LairezJ Pelta
Apr 28, 2009·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·C Le CoeurS Longeville
Aug 30, 2008·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·T BagnostC André
Dec 20, 2008·Journal of Pharmaceutical and Biomedical Analysis·L ExcoffonC André

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