A method to probe protein structure from UV absorbance spectra
Biter Amadeo B., Jeroen Pollet, Wen-Hsiang Chen, Ulrich Strych, Peter J. Hotez, Bottazzi, Maria Elena
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.
Circular dichroism, Tertiary structure, Protein folding, Protein denaturation, Biochemistry