title: L-Arginine increases the solubility of unfolded species of hen egg white lysozyme.
abstract: L-Arginine (L-Arg) has been widely used as an enhancer of protein renaturation. The mechanism behind its action is still not fully understood. Using hen egg white lysozyme as a model protein, we present data that clearly demonstrate the suppression of the aggregation of denatured protein by L-Arg. By chemical modification of free cysteines, a series of unfolded lysozyme species were obtained that served as models for unfolded and intermediate states during the process of oxidative refolding. An increased equilibrium solubility of unfolded species and intermediates in the presence of L-Arg seems to be its major mechanism of action.
authors.affiliation: Institut für Biotechnologie, Martin-Luther-Universität Halle/Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle (Saale), Germany.
authors.forename: Ravi Charan
authors.initials: RC
authors.lastname: Reddy K
authors.forename: Hauke
authors.initials: H
authors.lastname: Lilie
authors.forename: Rainer
authors.initials: R
authors.lastname: Rudolph
authors.forename: Christian
authors.initials: C
authors.lastname: Lange
mesh_terms: D001120:Arginine / Q000494:pharmacology*; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding; D020673:Protein Renaturation / Q000187:drug effects; D012995:Solubility
chemical_list: D001120:Arginine; C421864:hen egg lysozyme; D009113:Muramidase
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