Unknown

Dataset Information

0

Coiled-Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection.


ABSTRACT: 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.

SUBMITTER: Mueller C 

PROVIDER: S-EPMC6391972 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Coiled-Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection.

Mueller Carolin C   Grossmann Tom N TN  

Angewandte Chemie (International ed. in English) 20181128 52


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 hai  ...[more]

Similar Datasets

| S-EPMC5916467 | biostudies-literature
| S-EPMC6485442 | biostudies-literature
| S-EPMC4744968 | biostudies-literature
| S-EPMC7182445 | biostudies-literature
| S-EPMC9452514 | biostudies-literature
| S-EPMC5113151 | biostudies-literature
| S-EPMC10127268 | biostudies-literature
| S-EPMC7496730 | biostudies-literature
| S-EPMC1868409 | biostudies-literature
| S-EPMC395749 | biostudies-literature