title: Understanding how proteins fold: the lysozyme story so far.
abstract: Hen lysozyme is one of the best characterized and most studied of all proteins. Recently, we have used a range of different methods to examine the events involved in the in vitro folding pathway of this protein. In this review we show that, by combining complementary techniques, it has been possible to piece together a detailed model for the folding of this enzyme. Important questions prompted by this work are highlighted and we then propose some ideas consistent with our data, as well as those of others, which we believe begin to provide insight into one of the most intriguing of structural problems in biology--how proteins can achieve their complex native forms from disordered denatured states.
authors.affiliation: Oxford Centre for Molecular Sciences, University of Oxford, UK.
authors.forename: C M
authors.initials: CM
authors.lastname: Dobson
authors.forename: P A
authors.initials: PA
authors.lastname: Evans
authors.forename: S E
authors.initials: SE
authors.lastname: Radford
mesh_terms: D000818:Animals; D002645:Chickens; D004578:Electron Spin Resonance Spectroscopy; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D009113:Muramidase