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. © 2012 Springer Science+Business Media, LLC.