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Protein folding and aggregation studied by isoelectric focusing across a urea gradient and isoelectric focusing in
P J van den Oetelaar1, B M de Man, H J Hoenders
1Department of Biochemistry, University of Nijmegen, The Netherlands.
Abstract:
Isoelectric focusing across a concentration gradient of urea was used to study the folding-unfolding and association-dissociation processes of proteins. Myoglobulin, albumin, RNase, papain, beta L- and alpha-crystallin were analyzed with this technique, and examples are given of visualized dissociation steps and of equilibrium-unfolding intermediates. Furthermore, a two-dimensional isoelectric focusing technique is presented that is useful to deduce whether a transition of a protein aggregate observed upon urea-gradient isoelectric focusing must be attributed to a change in the protein's tertiary or quaternary structure.