title: [De novo proteins with a given spatial structure: new approaches to design and analysis].
abstract: Based on the molecular theory of protein structure the de novo protein was designed in order to obtain the tertiary fold which has not yet been observed in natural proteins, namely four-stranded antiparallel beta-sheet covered by two alpha-helixes. The gene coding for this protein (named albebetin) was chemically synthesized, cloned in plasmid with SP6 phage promoter and expressed in mRNA-dependent cell-free translation system. An approach was developed to study albebetin using only nanogram amounts of radio labelled protein without previous purification. The preliminary analysis of its structure by gel-filtration, urea-gradient electrophoresis and limited proteolysis revealed compactness and stability of the de novo protein.
authors: D A
authors: DA
authors: Dolgikh
authors: M P
authors: MP
authors: Kirpichnikov
authors: O B
authors: OB
authors: Ptitsyn
authors: A N
authors: AN
authors: Fedorov
authors: A V
authors: AV
authors: Finkel'shteĭn
authors: V V
authors: VV
authors: Chemeris
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D010957:Plasmids; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012333:RNA, Messenger / Q000378:metabolism
chemical_list: D011506:Proteins; D012333:RNA, Messenger; C074146:albebetin
vernacular_title: Belok de novo s zadannoĭ prostranstvennoĭ strukturoĭ: novye podkhody k konstruirovaniiu i analizu.