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Coiled‐Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection
Author(s) -
Mueller Carolin,
Grossmann Tom N.
Publication year - 2018
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201811515
Subject(s) - coiled coil , folding (dsp implementation) , biophysics , intramolecular force , chemistry , peptide , conformational change , protein folding , random coil , epitope , biochemistry , stereochemistry , protein secondary structure , biology , genetics , antigen , electrical engineering , engineering
The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled‐coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled‐coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin‐like conformation that opens upon receptor binding. Variation of the coiled‐coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real‐time.