title: How important is the molten globule for correct protein folding?
abstract: The molten globule (MG) state is widely considered to be an important intermediate in protein folding and to have a polypeptide backbone with a native-like topology. The experimental evidence for this view was obtained largely, however, with MG proteins containing native-like constraints. When the four disulphide bonds of alpha-lactalbumin were allowed to rearrange to those favoured by the MG, opposite conclusions were obtained. Consideration of all the experimental data indicates that any tendency of this MG to be native-like is negligible relative to all the other topologies that it can adopt. Furthermore, the experimental data indicate that the MG is not the key to rapid protein folding.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, Germany. creighton@embl-heidelberg.de
authors.forename: T E
authors.initials: TE
authors.lastname: Creighton
mesh_terms: D004220:Disulfides / Q000737:chemistry; D007768:Lactalbumin / Q000737:chemistry; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D004220:Disulfides; D007768:Lactalbumin