title: The role of proline in the prevention of aggregation during protein folding in vitro.
abstract: Proline effectively inhibits protein aggregation during the refolding of bovine carbonic anhydrase. Other osmolytes used such as glycine and ethylene glycol fail to exhibit the 'aggregation-blockade' role shown by proline. Results of viscosity and ANS fluorescence (1-anilino-8-naphthalene sulphonic acid) experiments suggest that proline at high concentrations forms an ordered supramolecular assembly. Based on these results, it is proposed that proline behaves as a protein folding chaperone due to the formation of an ordered, amphipathic supramolecular assembly. To our knowledge, this is the first report wherein proline is proposed as a protein folding aid.
authors.affiliation: Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan.
authors.forename: T K
authors.initials: TK
authors.lastname: Kumar
authors.forename: D
authors.initials: D
authors.lastname: Samuel
authors.forename: G
authors.initials: G
authors.lastname: Jayaraman
authors.forename: T
authors.initials: T
authors.lastname: Srimathi
authors.forename: C
authors.initials: C
authors.lastname: Yu
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D000818:Animals; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D019855:Ethylene Glycol / Q000494:pharmacology; D005456:Fluorescent Dyes / Q000378:metabolism; D005998:Glycine / Q000494:pharmacology; D018832:Molecular Chaperones / Q000494:pharmacology; D011392:Proline / Q000737:chemistry / Q000494:pharmacology*; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D014783:Viscosity
chemical_list: D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D018832:Molecular Chaperones; C027132:1-anilino-8-naphthalenesulfonate; D011392:Proline; D002256:Carbonic Anhydrases; D019855:Ethylene Glycol; D005998:Glycine