Fluorescence Quenching to Study Protein-ligand Binding: Common Errors

A number of recent articles, amongst others several published in the Journal of Fluorescence, use inappropriate fluorescence methodology to determine ligand binding characteristics to (mostly) proteins. In this Letter, several common pitfalls are discussed in relation to two recent publications in t...

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Bibliographic Details
Published inJournal of fluorescence Vol. 20; no. 2; pp. 625 - 629
Main Author van de Weert, Marco
Format Journal Article
LanguageEnglish
Published Boston Springer US 01.03.2010
Subjects
Algorithms
Analytical Chemistry
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biomedicine
Biophysics
Biotechnology
Fluorescence Resonance Energy Transfer - methods
Ligands
Protein Binding
Protein Conformation
Proteins - chemistry
Short Communication
Signal Processing, Computer-Assisted
Spectrometry, Fluorescence - methods
Ligand binding
FRET
Inner-filter effect
Fluorescence quenching
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Summary:A number of recent articles, amongst others several published in the Journal of Fluorescence, use inappropriate fluorescence methodology to determine ligand binding characteristics to (mostly) proteins. In this Letter, several common pitfalls are discussed in relation to two recent publications in the Journal of Fluorescence (Wang et al. (2009) 19:801–808; Ding et al. (2009) 19:783–791). The Author hopes that this contribution helps to prevent a further spread of the incorrect methodology, and results in a reappraisal of those articles already published using similar methodology.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Commentary-1
ISSN:1053-0509
1573-4994
DOI:10.1007/s10895-009-0572-x