Next Article in Journal
Insights into Vibrio parahaemolyticus CHN25 Response to Artificial Gastric Fluid Stress by Transcriptomic Analysis
Next Article in Special Issue
Rise-Time of FRET-Acceptor Fluorescence Tracks Protein Folding
Previous Article in Journal
Comprehensive Analysis of Neonatal versus Adult Unilateral Decortication in a Mouse Model Using Behavioral, Neuroanatomical, and DNA Microarray Approaches
Previous Article in Special Issue
Insulin Induces an Increase in Cytosolic Glucose Levels in 3T3-L1 Cells with Inhibited Glycogen Synthase Activation
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2014, 15(12), 22518-22538; doi:10.3390/ijms151222518

Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Department of Chemistry, Dongguk University, Seoul 100-715, Korea
*
Author to whom correspondence should be addressed.
Received: 8 October 2014 / Revised: 8 November 2014 / Accepted: 18 November 2014 / Published: 5 December 2014
(This article belongs to the Special Issue Förster Resonance Energy Transfer (FRET) 2015)
View Full-Text   |   Download PDF [461 KB, uploaded 5 December 2014]   |  

Abstract

F resonance energy transfer (FRET) occurs when the distance between a donor fluorophore and an acceptor is within 10 nm, and its application often necessitates fluorescent labeling of biological targets. However, covalent modification of biomolecules can inadvertently give rise to conformational and/or functional changes. This review describes the application of intrinsic protein fluorescence, predominantly derived from tryptophan (λEX ∼ 280 nm, λEM ∼ 350 nm) , in protein-related research and mainly focuses on label-free FRET techniques. In terms of wavelength and intensity, tryptophan fluorescence is strongly influenced by its (or the proteinlocal environment, which, in addition to fluorescence quenching, has been applied to study protein conformational changes. Intrinsic F resonance energy transfer (iFRET), a recently developed technique, utilizes the intrinsic fluorescence of tryptophan in conjunction with target-specific fluorescent probes as FRET donors and acceptors, respectively, for real time detection of native proteins. View Full-Text
Keywords: FRET; label free detection; tryptophan fluorescence; intrinsic fluorescence; protein imaging; biosensors; immunoassay FRET; label free detection; tryptophan fluorescence; intrinsic fluorescence; protein imaging; biosensors; immunoassay
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ghisaidoobe, A.B.T.; Chung, S.J. Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques. Int. J. Mol. Sci. 2014, 15, 22518-22538.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top