title: Intrinsic fluorescence of intrinsically disordered proteins.
abstract: Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions. Indeed, the multidimensional character of fluorescence can provide information on local chemical features, on solvent diffusional processes, and on rotational movements of peptide chains or whole proteins. Here, we describe the details of quenching fluorescence experiments and how to correlate the results to the peculiar structural information on the organization of intrinsically disordered proteins (IDPs).
authors: Department of Biochemistry "G. Moruzzi", University of Bologna, Rimini, Italy.
authors: Paolo
authors: P
authors: Neyroz
authors: Stefano
authors: S
authors: Ciurli
mesh_terms: D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D028044:Phosphate-Binding Proteins; D011487:Protein Conformation; D011489:Protein Denaturation; D012984:Software; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D028044:Phosphate-Binding Proteins; C082270:ureG protein, Bacteria; D014364:Tryptophan