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  4. Mapping the binding sites of peptide and non-peptide molecules to G protein-coupled receptors by fluorescence
 
research article

Mapping the binding sites of peptide and non-peptide molecules to G protein-coupled receptors by fluorescence

Chollet, A.
•
Turcatti, G.  
1998
Letters in Peptide Science

Novel fluorescence approaches to investigate ligand recognition and structure of G protein-coupled receptors in native membranes have been developed. These methods combine the biosynthetic incorporation of unnatural fluorescent amino acids at known sites in receptors with the technique of fluorescence energy transfer for distance measurement. This permits one to fix the ligand in space and to define the structure of the receptor in a model of ligand-receptor interactions. Subdomains of ligand binding sites on NK1 and NK2 receptors were also characterized using environment-sensitive fluorophores and the techniques of collisional quenching and anisotropy. Antagonists and agonists have different binding sites on NK1 and NK2.

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Type
research article
DOI
10.1007/BF02443443
Author(s)
Chollet, A.
Turcatti, G.  
Date Issued

1998

Published in
Letters in Peptide Science
Volume

5

Issue

2-3

Start page

79

End page

82

Subjects

Fluorescence resonance energy transfer (FRET)

•

Ligand-receptor interactions

•

Neurokinin receptors

•

Nonsense suppression mutagenesis

Editorial or Peer reviewed

REVIEWED

Written at

OTHER

EPFL units
PTCB  
Available on Infoscience
August 14, 2006
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/232865
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