title: Modification tolerability of soybean proglycinin.
abstract: Proglycinins containing multiple modifications, that is, with two kinds of single modifications, designed previously to improve food functions, were assessed for ability to form proper conformations. This was done to discover the modification tolerability of proglycinin. Based on our results, three new criteria are proposed for judging formation of proper conformations. Our results suggest that proglycinin molecules tolerate different combinations of single modifications without misfolding.
authors.affiliation: Research Institute for Food Science, Kyoto University, Japan.
authors.forename: A B
authors.initials: AB
authors.lastname: Gidamis
authors.forename: P
authors.initials: P
authors.lastname: Wright
authors.forename: Z U
authors.initials: ZU
authors.lastname: Haque
authors.forename: T
authors.initials: T
authors.lastname: Katsube
authors.forename: M
authors.initials: M
authors.lastname: Kito
authors.forename: S
authors.initials: S
authors.lastname: Utsumi
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli; D005916:Globulins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D017510:Protein Folding; D011498:Protein Precursors; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012995:Solubility; D030262:Soybean Proteins; D013025:Glycine max / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D005916:Globulins; D010940:Plant Proteins; D011498:Protein Precursors; D011993:Recombinant Fusion Proteins; D030262:Soybean Proteins; C011474:glycinin