Steady-state fluorescence quenching applications for studying protein structure and dynamics

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Abstract

Fluorescence quenching methods are useful to obtain information about the conformational and/or dynamic changes of proteins in complex macromolecular systems. In this review steady-state methods are described and the data interpretation is thoroughly discussed. As a special case of fluorescence quenching mechanism, fluorescence resonance energy transfer (FRET) phenomenon is also presented. Application of a FRET based method to characterize the temperature dependence of the flexibility of protein matrix is clearly demonstrated.

Original languageEnglish
Pages (from-to)223-236
Number of pages14
JournalJournal of Photochemistry and Photobiology, B: Biology
Volume83
Issue number3
DOIs
Publication statusPublished - Jun 1 2006

Fingerprint

resonance fluorescence
protein structure
Quenching
Fluorescence Resonance Energy Transfer
Fluorescence
energy transfer
quenching
fluorescence
proteins
Proteins
complex systems
Large scale systems
Multiprotein Complexes
flexibility
multiprotein complexes
temperature dependence
matrices
Temperature
methodology
temperature

Keywords

  • Fluorescence quenching
  • FRET
  • Protein structure
  • Tryptophan fluorescence

ASJC Scopus subject areas

  • Plant Science
  • Bioengineering
  • Physical and Theoretical Chemistry

Cite this

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KW - Tryptophan fluorescence

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