Final answer:
Aromatic amino acids absorb UV light at peak wavelengths between 260 nm to 290 nm, which can be analyzed using UV spectroscopy to study protein structure and conformational changes.
Step-by-step explanation:
The aromatic amino acids, which include tryptophan, phenylalanine, and tyrosine, can absorb ultraviolet (UV) light within a specific range of wavelengths.
They have a characteristic absorbance peak between 260 nm to 290 nm, which is within the UV range. These amino acids are chromophores due to their conjugated pi-bonding systems, which allow them to absorb light at these wavelengths.
The Beer-Lambert Law can be applied using UV spectroscopy to determine the concentration of a chromophore by correlating the absorbance at a particular wavelength with its concentration.
This is a vital principle in organic and biological chemistry where UV-Vis spectroscopy plays a crucial role in studying molecular structures such as proteins and their conformational changes; such changes can alter the UV absorbance of the aromatic amino acid residues.