title: Secondary structure of human interleukin-3.
abstract: 1. The secondary structure of human interleuken-3 in solution was determined by circular dichroism spectroscopy. 2. The results were then compared with empirical secondary structure predictions based on primary sequence structure of the protein. 3. The two approaches are in extremently close agreement showing the protein to have 40% alpha-helix, 12% total beta-structure and 48% random coil content.
authors.affiliation: Monsanto Corporate Research, Monsanto Company, St. Louis, MO 63198.
authors.forename: J J
authors.initials: JJ
authors.lastname: Freeman
authors.forename: G R
authors.initials: GR
authors.lastname: Parr
authors.forename: R I
authors.initials: RI
authors.lastname: Hecht
authors.forename: J C
authors.initials: JC
authors.lastname: Morris
authors.forename: J P
authors.initials: JP
authors.lastname: McKearn
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D006801:Humans; D007377:Interleukin-3 / Q000737:chemistry*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D007377:Interleukin-3; D011994:Recombinant Proteins