Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques
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...
Main Authors: | Amar B. T. Ghisaidoobe, Sang J. Chung |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2014-12-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | http://www.mdpi.com/1422-0067/15/12/22518 |
Similar Items
-
Quantum dot-fluorescent protein pairs as fluorescence resonance energy transfer pairs
by: Dennis, Allison Marie
Published: (2011) -
Fluorescent Proteins as Genetically Encoded FRET Biosensors in Life Sciences
by: Bernhard Hochreiter, et al.
Published: (2015-10-01) -
Rapid and Simple Detection of Ochratoxin A using Fluorescence Resonance Energy Transfer on Lateral Flow Immunoassay (FRET-LFI)
by: Hyun-Kyung Oh, et al.
Published: (2019-05-01) -
A Guide to Fluorescent Protein FRET Pairs
by: Bryce T. Bajar, et al.
Published: (2016-09-01) -
Quantitative analysis of Förster resonance energy transfer from spectrally resolved fluorescence measurements
by: Woehler, Andrew T.
Published: (2010)