FRET events in fluorescent pentapeptides containing aliphatic triazolo amino acid scaffolds: Role of spacer lengths-Science-Chemical Encyclopedia-lookchem

FRET events in fluorescent pentapeptides containing aliphatic triazolo amino acid scaffolds: Role of spacer lengths
Add time:07/24/2019 Source:sciencedirect.com

The FRET efficiencies in donor/acceptor pairs in the two termini of designed fluorescent pentapeptides depend on the flexibility of two arms of triazolyl amino acid scaffolds positioned in the center of the backbones inducing predominant β-sheet conformations. Flexible N-Terminus of the scaffold in a pentapeptide has led to higher FRET efficiency and makes it different from other peptide with flexible C-terminus.

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