Ontology highlight
ABSTRACT:
SUBMITTER: Goldberg JM
PROVIDER: S-EPMC3360930 | biostudies-literature | 2012 Apr
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20120403 14
Fluorescent probe pairs that can be selectively excited in the presence of Trp and Tyr are of great utility in studying conformational changes in proteins. However, the size of these probe pairs can restrict their incorporation to small portions of a protein sequence where their effects on secondary and tertiary structure can be tolerated. Our findings show that a thioamide bond-a single atom substitution of the peptide backbone-can quench fluorophores that are red-shifted from intrinsic protein ...[more]