title: Recent progress in NMR spectroscopy: toward the study of intrinsically disordered proteins of increasing size and complexity.
abstract: Thanks to recent fast progress, NMR is now in a strategic position to provide unique atomic resolution information on a variety of different biological macromolecules in different conditions (solution, solid state, in-cell). We would like here to present recent developments that enable to focus on intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs) of proteins of increasing size and complexity. They have attracted the attention of the scientific community challenging well accepted ideas and concepts and demanding an expansion of the structure function paradigm.
authors.affiliation: CERM and Department of Chemistry Ugo Schiff, University of Florence, Sesto Fiorentino, Italy. felli@cerm.unifi.it
authors.forename: Isabella C
authors.initials: IC
authors.lastname: Felli
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
mesh_terms: D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory
chemical_list: D011506:Proteins