NDLI: Observation of protein folding/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET

Content Provider	Springer Nature Link
Author	Yang, Li Ling Kao, Michael W. P. Chen, Hsin Liang Lim, Tsong Shin Fann, Wunshain Chen, Rita P. Y.
Copyright Year	2011
Abstract	A ubiquitin mutant with two Cys mutations, m[C]q/S65C, was site-specifically labeled with two dye molecules, Alexa Fluor 488 (donor) and Alexa Fluor 594 (acceptor), due to the different reactivity of these two Cys residues. This doubly dye-labeled ubiquitin has lower structural stability than wild-type ubiquitin. Taking advantage of this decreased stability, conformational heterogeneity of this protein under nondenaturing condition was observed at the single-molecule level using single-paired Förster resonance energy transfer (FRET) by trapping the protein in agarose gel. Three conformational populations corresponding to folded (E ET ≈ 0.95), loosely packed (E ET ≈ 0.72), and unfolded (E ET ≈ 0.22) structures, and the structural transitions between them were observed. Our results suggest that agarose immobilization is good for observing structural dynamics of proteins under native condition.
Starting Page	189
Ending Page	198
Page Count	10
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	41
Issue Number	2
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-11-09
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	FRET Ubiquitin Folding Single molecule Conformational heterogeneity Agarose Membrane Biology Biophysics and Biological Physics Nanotechnology Biochemistry Neurobiology Cell Biology
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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