title: Folding of bovine growth hormone is consistent with the molten globule hypothesis.
abstract: Previous results from equilibrium and kinetic studies of the folding of bovine growth hormone (bGH) have demonstrated that bGH does not follow a simple two-step folding mechanism. These results are summarized and interpreted according to the "molten globule" model. The molten globule state of bGH is characterized as a folding intermediate which is largely alpha-helical, retains a compact hydrodynamic radius, has packing of the aromatic side chains that is similar to the unfolded state, and possesses a solvent-exposed hydrophobic surface along helix 106-127 that readily leads to association.
authors.affiliation: Control R & D, Upjohn Company, Kalamazoo, Michigan 49001.
authors.forename: D N
authors.initials: DN
authors.lastname: Brems
authors.forename: H A
authors.initials: HA
authors.lastname: Havel
mesh_terms: D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004926:Escherichia coli / Q000032:analysis; D013006:Growth Hormone / Q000032:analysis*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000032:analysis; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
chemical_list: D011994:Recombinant Proteins; D013006:Growth Hormone