title: Redesigning a sweet protein: increased stability and renaturability.
abstract: Monellin is one of two natural proteins from African berries with potent sweet taste. Monellin is the smaller of the two, and consists of two peptides. The protein loses sweetness when heated above 50 degrees C under acidic pH. Based on the crystal structure of monellin we have fused the two chains into a single chain using several different linkers copied and 'transplanted' from the same molecule. One of the newly designed proteins is as potently sweet as the natural one, is more stable upon temperature or pH changes, and renatures easily even after heating to 100 degrees C at low pH.
authors: Department of Chemistry, University of California, Berkeley 94720.
authors: S H
authors: SH
authors: Kim
authors: C H
authors: CH
authors: Kang
authors: R
authors: R
authors: Kim
authors: J M
authors: JM
authors: Cho
authors: Y B
authors: YB
authors: Lee
authors: T K
authors: TK
authors: Lee
mesh_terms: D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification; D013696:Temperature
chemical_list: D010940:Plant Proteins; D011994:Recombinant Proteins; C002541:monellin protein, Dioscoreophyllum cumminsii