4 Dynamic quenching is described by the Stern-Volmer mechanism and results by collisions of the excited state molecule with the quencher. Since thioamide analogs of the natural amino acids can be synthetically incorporated into peptides, they can function as minimally-perturbing probes of protein/peptide interactions. A second type of quenching mechanism, termed static or complex quenching, arises from non-fluorescent complexes formed between the quencher and fluorophore that serve to limit absorption by reducing the population of active, excitable molecules. As said in the section on the Stokes shift, fluorescence is a very sensitive method for studying the local environment around the fluorophore. This is a trivial type of quenching which contains little molecular information. Fluorescence quenching can also take place by the formation at the ground state of a non-fluorescent complex. Fluorescence quenching is a physicochemical process that lowers the intensity of emitted light from fluorescent molecules. Quenching of 2 -aminopurine fluorescence in DNA is dominated by distance-dependent electron transfer from 2 -aminopurine to guanosine [2]. The order of quenching efficiency is G

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