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Thioamide quenching of intrinsic protein fluorescence.


ABSTRACT: Thioamides quench tryptophan and tyrosine fluorescence in a distance-dependent manner and thus can be used to monitor the binding of thioamide-containing peptides to proteins. 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.

SUBMITTER: Goldberg JM 

PROVIDER: S-EPMC7759719 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Thioamide quenching of intrinsic protein fluorescence.

Goldberg Jacob M JM   Wissner Rebecca F RF   Klein Alyssa M AM   Petersson E James EJ  

Chemical communications (Cambridge, England) 20110912 10


Thioamides quench tryptophan and tyrosine fluorescence in a distance-dependent manner and thus can be used to monitor the binding of thioamide-containing peptides to proteins. 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. ...[more]

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