title: A stabilized molten globule protein.
abstract: A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling. This unique isomer retains a substantial content of alpha-helical structure. It is stabilized by two native disulfide bonds within the alpha-helical domain and two scrambled non-native disulfide bonds at the beta-sheet domain. This denatured isomer of alpha-LA exhibits structural characteristics that are consistent with the well-documented molten globule state. The ability to prepare a stabilized and structurally defined molten globule provides a useful model for studying the folding and unfolding pathways of proteins.
authors.affiliation: Research Center for Protein Chemistry, Institute of Molecular Medicine and the Department of Biochemistry and Molecular Biology, University of Texas, 2121 W. Holcombe Blvd., Houston, TX 77030, USA.
authors.forename: J
authors.initials: J
authors.lastname: Chang
authors.forename: A
authors.initials: A
authors.lastname: Bulychev
authors.forename: L
authors.initials: L
authors.lastname: Li
mesh_terms: D002942:Circular Dichroism; D004220:Disulfides; D004355:Drug Stability; D006358:Hot Temperature; D007768:Lactalbumin / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D020033:Protein Isoforms / Q000737:chemistry; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D004220:Disulfides; D020033:Protein Isoforms; D007768:Lactalbumin