+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Fluorescence resonance energy transfer dynamics during protein folding: Evidence of multistage folding kinetics

Fluorescence resonance energy transfer dynamics during protein folding: Evidence of multistage folding kinetics

Current Science 85(1): 68-72, 10 July

Fluorescence resonance energy transfer (FRET) during folding of a model protein, HP-36, is investigated by Brownian dynamics simulation. Computer simulations of this protein show that folding kinetics is non-exponential and multistage, after a fast initial hydrophobic collapse. This multistage dynamics can be captured in FRET with a suitably chosen donor-acceptor pair. In particular, we find that FRET can be sensitive to late stages of changes in the radius of gyration which is found to occur for this model protein. This late stage dynamics is driven by changes in the topological pair contact formation.

(PDF emailed within 1 workday: $29.90)

Accession: 012095668

Download citation: RISBibTeXText

Related references

Probing protein folding dynamics via fluorescence-energy-transfer kinetics. Abstracts of Papers American Chemical Society 224(1-2): PHYS 264, 2002

An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for "double kinetics" experiments: application to fluorescence resonance excitation energy transfer study of protein folding. Review of Scientific Instruments 83(8): 084301, 2013

RNA folding dynamics by single-molecule fluorescence resonance energy transfer. Methods 49(2): 112-117, 2009

Two-dimensional fluorescence resonance energy transfer as a probe for protein folding: a theoretical study. Journal of Chemical Physics 128(11): 115102, 2008

Simulation of fluorescence resonance energy transfer experiments: effect of the dyes on protein folding. Journal of Physics. Condensed Matter 22(23): 235103, 2011

The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer. Febs Letters 579(4): 916-920, 2005

Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: temperature-/urea-dependent folding kinetics and thermodynamics. Journal of Physical Chemistry. B 118(14): 3853-3863, 2015

Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. Proceedings of the National Academy of Sciences of the United States of America 97(10): 5179-5184, 2000

Microsecond protein folding events revealed by time-resolved fluorescence resonance energy transfer in a microfluidic mixer. Analytical Chemistry 87(11): 5589-5595, 2015

Extracting the single-molecule fluorescence trajectories of folding protein in single-pair fluorescence resonance energy transfer experiment. Journal of Nanoscience and Nanotechnology 9(2): 1176-1180, 2009

RNA conformation and folding studied with fluorescence resonance energy transfer. Methods 23(3): 240-254, 2001

Quantification of Millisecond Protein-Folding Dynamics in Membrane-Mimetic Environments by Single-Molecule Förster Resonance Energy Transfer Spectroscopy. Analytical Chemistry 87(22): 11224-11232, 2016

The structure and folding of branched RNA analyzed by fluorescence resonance energy transfer. Methods in Enzymology 469: 159-187, 2011

Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape. Protein Science 18(1): 58-68, 2009

Ion-induced folding of the hammerhead ribozyme: a fluorescence resonance energy transfer study. Embo Journal 16(24): 7481-7489, 1998