Tyrosine ionic properties

The aromatic rings in the protein absorb ultraviolet light at an absorbance maximum of 280 nm, whereas the peptide bonds absorb at around 205 nm. The unique absorbance property of proteins could be used to estimate the level of proteins. These methods are fairly accurate with the ranges from 20 p,g to 3 mg for absorbance at 280 nm, as compared with 1 to 100 p,g for 205 nm. The assay is non-destructive as the protein in most cases is not consumed and can be recovered. Secondary, tertiary and quaternary structures all affect absorbance therefore, factors such as pH, ionic strength, etc can alter the absorbance spectrum. This assay depends on the presence of a mino acids which absorb UV light (mainly tryptophan, but to a lesser extent also tyrosine). Small peptides that do not contain such a mino acids cannot be measured easily by UV. 

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