title: Improving the soluble expression of recombinant proteins by randomly shuffling 5' and 3' coding-sequence ends.
abstract: Many structural genomics (SG) programmes rely on the design of soluble protein domains. The production and screening of large libraries to experimentally select these soluble protein-encoding constructs are limited by the technologies and efforts that can be devoted to a single target. Using basic technologies available in any laboratory, a method named `boundary shuffling' was devised to generate orientated libraries for soluble domain selection without impeding the target flow.
authors: Aix-Marseille Université, CNRS, AFMB UMR 7257, 13288 Marseille, France.
authors: Christophe
authors: C
authors: Bignon
authors: Changqing
authors: C
authors: Li
authors: Julie
authors: J
authors: Lichière
authors: Bruno
authors: B
authors: Canard
authors: Bruno
authors: B
authors: Coutard
mesh_terms: D000595:Amino Acid Sequence; D023281:Genomics; D016752:Hepatitis E virus / Q000737:chemistry*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry*; D012995:Solubility; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D011994:Recombinant Proteins; D014764:Viral Proteins
keywords: boundary shuffling; soluble protein domains