Paper
9 July 1999 Mag-Indo-1 protein interaction as a tool for probing the 3D conformation of protein subdomains: influence of the chemical microenvironment of the histidin residue(s) on the paramaters of the intera
Pierre M. Viallet, Tuan Vo-Dinh, Terry Bunde, Anne-Cecile Ribou, Jean Vigo, Jean-Marie Salmon
Author Affiliations +
Proceedings Volume 3595, Biomedical Diagnostic, Guidance, and Surgical-Assist Systems; (1999) https://doi.org/10.1117/12.351536
Event: BiOS '99 International Biomedical Optics Symposium, 1999, San Jose, CA, United States
Abstract
Magnesium complexation with Mag-indo-1 results in a shift of the emission fluorescence spectrum from 480 nm to 417 nm. Mag-indo-1 is also able to bind calcium and zinc. These cationic interactions induce the same spectral shift but the fluorescence intensity and the dissociation constant are dependent of the nature of the cation. Furthermore Mag-indo- 1 bind also proteins through a specific interaction with some histidin residues. That interaction induces a characteristic spectral shift of the emission fluorescence spectra from 480 to 457 nM.
© (1999) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Pierre M. Viallet, Tuan Vo-Dinh, Terry Bunde, Anne-Cecile Ribou, Jean Vigo, and Jean-Marie Salmon "Mag-Indo-1 protein interaction as a tool for probing the 3D conformation of protein subdomains: influence of the chemical microenvironment of the histidin residue(s) on the paramaters of the intera", Proc. SPIE 3595, Biomedical Diagnostic, Guidance, and Surgical-Assist Systems, (9 July 1999); https://doi.org/10.1117/12.351536
Lens.org Logo
CITATIONS
Cited by 1 scholarly publication.
Advertisement
Advertisement
RIGHTS & PERMISSIONS
Get copyright permission  Get copyright permission on Copyright Marketplace
KEYWORDS
Luminescence

Proteins

Energy transfer

Calcium

Magnesium

Molecules

Molecular energy transfer

Back to Top