title: Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.
abstract: Fibronectin type III modules contain approximately 90 residues and are an extremely common building block of animal proteins. Despite containing a complex all-beta-sheet topology and eight prolines, the refolding of the 10th type III module of human fibronectin has been found to be very rapid, with native core packing, amide hydrogen bonding, and backbone conformation all recovered within 1 s at 5 degrees C. These observations indicate that this domain can overcome many structural characteristics often thought to slow the folding process.
authors.affiliation: Oxford Centre for Molecular Sciences, University of Oxford, England.
authors.forename: K W
authors.initials: KW
authors.lastname: Plaxco
authors.forename: C
authors.initials: C
authors.lastname: Spitzfaden
authors.forename: I D
authors.initials: ID
authors.lastname: Campbell
authors.forename: C M
authors.initials: CM
authors.lastname: Dobson
mesh_terms: D002942:Circular Dichroism; D005353:Fibronectins / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins; D012995:Solubility
chemical_list: D005353:Fibronectins; D011994:Recombinant Proteins