title: Recombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks.
abstract: The growing recognition of the several roles that intrinsically disordered proteins play in biology places an increasing importance on protein sample availability to allow the characterization of their structural and dynamic properties. The sample preparation is therefore the limiting step to allow any biophysical method being able to characterize the properties of an intrinsically disordered protein and to clarify the links between these properties and the associated biological functions. An increasing array of tools has been recruited to help prepare and characterize the structural and dynamic properties of disordered proteins. This chapter describes their sample preparation, covering the most common drawbacks/barriers usually found working in the laboratory bench. We want this chapter to be the bedside book of any scientist interested in preparing intrinsically disordered protein samples for further biophysical analysis.
authors.affiliation: Magnetic Resonance Center (CERM), University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy. eocalcada@gmail.com.
authors.forename: Eduardo O
authors.initials: EO
authors.lastname: Calçada
authors.affiliation: Giotto Biotech, Via Madonna del Piano 6, 50019, Sesto Fiorentino, Italy. korsak@giottobiotech.com.
authors.forename: Magdalena
authors.initials: M
authors.lastname: Korsak
authors.affiliation: Giotto Biotech, Via Madonna del Piano 6, 50019, Sesto Fiorentino, Italy. kozyreva@giottobiotech.com.
authors.forename: Tatiana
authors.initials: T
authors.lastname: Kozyreva
mesh_terms: D019295:Computational Biology; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010957:Plasmids; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D064267:Intrinsically Disordered Proteins; D011994:Recombinant Proteins
keywords: Heat-stable proteins; Hydrodynamic volume; Isotope labeling; Isotopic enrichment; Protein expression; Protein purification; Protein solubility; Protein tags; Purification; Recombinant expression