643018-84-2Relevant academic research and scientific papers
Tryptophan-based fluorophores for studying protein conformational changes
Talukder, Poulami,Chen, Shengxi,Liu, C. Tony,Baldwin, Edwin A.,Benkovic, Stephen J.,Hecht, Sidney M.
, p. 5924 - 5934 (2015/01/09)
With the continuing interest in deciphering the interplay between protein function and conformational changes, small fluorescence probes will be especially useful for tracking changes in the crowded protein interior space. Presently, we describe the poten
Minimalist probes for studying protein dynamics: Thioamide quenching of selectively excitable fluorescent amino acids
Goldberg, Jacob M.,Speight, Lee C.,Fegley, Mark W.,Petersson, E. James
, p. 6088 - 6091 (2012/05/07)
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 prot
Synthesis of N-[(tert-Butoxy)carbonyl]-3-(9,10-dihydro-9-oxoacridin-2-yl)-L-alanine, a New Fluorescent Amino Acid Derivative
Szymanska, Aneta,Wegner, Katarzyna,Lankiewicz, Leszek
, p. 3326 - 3331 (2007/10/03)
A simple synthesis of a new, highly fluorescent amino acid and of its protected derivative useful in peptide studies is described. The obtained derivative, N-[(tert-butoxy)carbonyl]-3-(9,10-dihydro-9-oxoacridin-2-yl)-L-alanine (6), shows intense long-wave absorption (above 360 nm) and emission (above 400 nm). The quantum yield of fluorescence of the investigated compound is very high, so it can serve as a sensitive analytical probe useful, e.g., in analysis of peptide conformations.
