Non-fluorescent transient states of tyrosine as a basis for label-free protein conformation and interaction studies.

ABSTRACT: The amino acids tryptophan, tyrosine, and phenylalanine have been extensively used for different label-free protein studies, based on the intensity, lifetime, wavelength and/or polarization of their emitted fluorescence. Similar to most fluorescent organic molecules, these amino acids can undergo transitions into dark meta-stable states, such as triplet and photo-radical states. On the one hand, these transitions limit the fluorescence signal, but they are also highly environment-sensitive and can offer an additional set of parameters, reflecting interactions, folding states, and immediate environments around the proteins. In this work, by analyzing the average intensity of tyrosine emission under different excitation modulations with the transient state monitoring (TRAST) technique, we ex

SUBMITTER: Bagheri N 

PROVIDER: S-EPMC10948778 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature