title: Conformational states of sunflower (Helianthus annuus) Helianthinin: effect of heat and pH.
abstract: The structure and solubility of helianthinin, the most abundant protein of sunflower seeds, was investigated as a function of pH and temperature. Dissociation of the 11S form (hexamer) into the 7S form (trimer) gradually increased with increasing pH from 5.8 to 9.0. High ionic strength (I = 250 mM) stabilizes the 11S form at pH > 7.0. Heating and low pH resulted in dissociation into the monomeric constituents (2-3S). Next, the 7S and 11S forms of helianthinin were isolated and shown to differ in their secondary and tertiary structure, and to have denaturation temperatures (T(d)) of 65 and 90 degrees C, respectively. Furthermore, the existence of two populations of the monomeric form of helianthinin with denaturation temperatures of 65 and 90 degrees C was described. This leads to the hypothesis that helianthinin can adopt two different conformational states: one with T(d) = 65 degrees C and a second with T(d) = 90 degrees C.
authors.affiliation: Agrotechnology and Food Innovations B.V., Wageningen, The Netherlands.
authors.forename: Sergio
authors.initials: S
authors.lastname: González-Pérez
authors.forename: Johan M
authors.initials: JM
authors.lastname: Vereijken
authors.forename: Karin B
authors.initials: KB
authors.lastname: Merck
authors.forename: Gerrit A
authors.initials: GA
authors.lastname: van Koningsveld
authors.forename: Harry
authors.initials: H
authors.lastname: Gruppen
authors.forename: Alphons G J
authors.initials: AG
authors.lastname: Voragen
mesh_terms: D055516:2S Albumins, Plant; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D055314:Seed Storage Proteins; D012995:Solubility
chemical_list: D055516:2S Albumins, Plant; D010940:Plant Proteins; D055314:Seed Storage Proteins