Journal
BIOPHYSICAL JOURNAL
Volume 84, Issue 6, Pages 3904-3916Publisher
CELL PRESS
DOI: 10.1016/S0006-3495(03)75118-2
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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.
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