title: A protein dissection study of a molten globule.
abstract: Proteins have many distinct tertiary folds (Richardson, J. S. (1981) Adv. Prot. Chem. 34, 167-339). The term tertiary fold refers to the spatial organization of secondary structure elements (alpha-helices and beta-strands). It is not known when, in the process of protein folding, a native tertiary fold emerges. Here, we show that the helical domain of human alpha-lactalbumin, in isolation, forms a molten globule with the same overall tertiary fold as that found in intact alpha-lactalbumin. Formation of this native-like fold does not require extensive, specific side-chain packing. Our results suggest that much of the information transfer from one-dimension to three-dimensions has occurred at the molten globule stage of protein folding.
authors.affiliation: Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge 02142.
authors.forename: Z Y
authors.initials: ZY
authors.lastname: Peng
authors.forename: P S
authors.initials: PS
authors.lastname: Kim
mesh_terms: D002942:Circular Dichroism; D006801:Humans; D007768:Lactalbumin / Q000737:chemistry*; D008027:Light; D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D012542:Scattering, Radiation; D013056:Spectrophotometry, Ultraviolet
chemical_list: D007768:Lactalbumin