Abstract

The ability to detect and study single proteins in their native state without the use of fluorescent labels is crucial for understanding the behavior and function of proteins in their natural environment. The contemporary used technique of fluorescence labeling can alter the structure and function of proteins, making it difficult to obtain accurate information about their behavior in vivo. The natural UV autofluorescence of proteins is a potential solution (excitation 250-290 nm, emission 320-360 nm), but it remains a challenge due to the low quantum yield and absorption cross-section of the emitters in UV.

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