Ontology highlight
ABSTRACT:
SUBMITTER: Wissner RF
PROVIDER: S-EPMC3721677 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20130417 17
We have recently shown that p-cyanophenylalanine (Cnf) and a thioamide can be used as a minimally perturbing Förster resonant energy transfer (FRET) pair to monitor protein conformation. We have also shown that thioamide analogues of natural amino acids can be incorporated into full-sized proteins through native chemical ligation. For intermolecular studies with Cnf/thioamide FRET pairs, Cnf can be incorporated into proteins expressed in Escherichia coli through unnatural amino acid mutagenesis ...[more]