Title
A method to probe protein structure from UV absorbance spectra
Author
Biter Amadeo B., Jeroen Pollet, Wen-Hsiang Chen, Ulrich Strych, Peter J. Hotez, Bottazzi, Maria Elena
Year
2019
Journal
Analytical Biochemistry
Abstract
Proteins primarily absorb UV light due to the presence of tryptophan, tyrosine, and phenylalanine residues, with absorbance maxima at 280, 275, and 258 nm, respectively. We now demonstrate that a simple value obtained by relating the absorbance at all three wavelengths, [A280/A275 + A280/A258], is a generally useful, robust, and sensitive probe of protein ‘foldedness’, and thus can be used to investigate unfolding, refolding, disulfide bonds, stability, buffer excipients, and even protein-protein and protein-ligand interactions.
Instrument
J-1500
Keywords
Circular dichroism, Tertiary structure, Protein folding, Protein denaturation, Biochemistry