title: The use of UV-Vis absorption spectroscopy for studies of natively disordered proteins.
abstract: Absorption spectroscopy can be used to monitor structural changes upon transitions from ordered to disordered state in proteins. Changes in environment of tryptophan, tyrosine, and phenylalanine residues result in changes of their absorption spectra. In most cases the changes are small and can be measured only in a differential mode.
authors: Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow Region, Russia. epermyak@yandex.ru
authors: Eugene A
authors: EA
authors: Permyakov
mesh_terms: D000465:Algorithms; D010649:Phenylalanine / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D013056:Spectrophotometry, Ultraviolet; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
chemical_list: D011506:Proteins; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan