Which wavelength range corresponds to the emission of tryptophan fluorescence?

Tryptophan fluorescence is an important phenomenon in biochemistry, particularly when studying protein structure and dynamics. The correct wavelength range for the emission of tryptophan fluorescence is 310-355 nm. This range is significant because tryptophan is an amino acid with a unique side chain that allows it to absorb ultraviolet light and subsequently emit light in the specified range.

Fluorescence occurs when tryptophan absorbs light at shorter wavelengths (typically around 280 nm) and then re-emits that energy at longer wavelengths. The emission spectrum of tryptophan is primarily influenced by its environment, such as the presence of solvent and neighboring amino acids, which can affect the exact peak emission wavelength.

Understanding this wavelength range is critical for techniques like fluorescence spectroscopy, which is commonly used for analyzing protein conformations and interactions. This knowledge is applicable in various biochemistry research scenarios, enabling scientists to draw conclusions about protein behavior based on fluorescence measurements.