title: Photoactivable amino acid bioisosteres and mass spectrometry: snapshots of in vivo 3D protein structures.
abstract: From folded to crosslinked proteins. A new promising photo-crosslinking/mass spectrometry method for the structural characterisation of folded proteins is highlighted. A reactive photo-leucine can clamp the front residues in β-turn and β-hairpin domains, thus allowing us to look into the specific native 3D structure of proteins.
authors.affiliation: Dipartimento di Scienze Fisiche e Chimiche, Università dell'Aquila e Consorzio INCA, Via Vetoio, Coppito, 67100 L'Aquila, Italy.
authors.forename: Claudio
authors.initials: C
authors.lastname: Iacobucci
authors.forename: Samantha
authors.initials: S
authors.lastname: Reale
authors.forename: Francesco
authors.initials: F
authors.lastname: De Angelis
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D055668:Photochemical Processes; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D014466:Ultraviolet Rays
chemical_list: D000596:Amino Acids; D010455:Peptides; D011506:Proteins