title: Structural basis of the stability of a lysozyme molten globule.
abstract: Hydrogen exchange measurements on equine lysozyme show that amides in three of the four major helices of the native protein are significantly protected in a molten globule state formed at pH 2. The pattern of protection within the different helices, however, varies significantly. Examination of the pattern in the light of the native structure indicates that the side chains of the protected residues form a compact cluster within the core of the protein. We suggest that such a core is present in the molten globule state, indicating the existence of substantial native-like interactions between hydrophobic residues. The formation of clusters of this type during the early stages of folding could be crucial to directing polypeptide chains to their native structures.
authors.affiliation: Oxford Centre for Molecular Sciences, University of Oxford, UK.
authors.forename: L A
authors.initials: LA
authors.lastname: Morozova
authors.forename: D T
authors.initials: DT
authors.lastname: Haynie
authors.forename: C
authors.initials: C
authors.lastname: Arico-Muendel
authors.forename: H
authors.initials: H
authors.lastname: Van Dael
authors.forename: C M
authors.initials: CM
authors.lastname: Dobson
mesh_terms: D000818:Animals; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013696:Temperature
chemical_list: D009113:Muramidase