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Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes
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10.1063/1.3284509
/content/aip/journal/jcp/132/3/10.1063/1.3284509
http://aip.metastore.ingenta.com/content/aip/journal/jcp/132/3/10.1063/1.3284509
View: Figures

Figures

Image of FIG. 1.
FIG. 1.

A schematic representation of a polymer chain containing monomers. The FRET dyes are assumed to be located at positions and along the chain. The distance between the two monomers fluctuates on a time scale associated with the monomer-dependent reconfiguration time .

Image of FIG. 2.
FIG. 2.

The reconfiguration time inferred from the fluctuations of the distance between monomers and strongly depends on the choice of the monomers. It is close to the Rouse time when the monomers are located near the chain ends.

Image of FIG. 3.
FIG. 3.

The reconfiguration time extracted from the fluctuations of the distance between monomers 0 and increases if a tail of length is attached to one of the monomers.

Image of FIG. 4.
FIG. 4.

Reconfiguration time inferred from FRET efficiency fluctuations as a function of the sequence separation between the donor and the acceptor. Inset: rms donor-acceptor separation as a function of .

Image of FIG. 5.
FIG. 5.

The reconfiguration time is determined by the folding/refolding time scales of the helix enclosed by A and B and thus can be much longer than .

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/content/aip/journal/jcp/132/3/10.1063/1.3284509
2010-01-21
2014-04-19
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes
http://aip.metastore.ingenta.com/content/aip/journal/jcp/132/3/10.1063/1.3284509
10.1063/1.3284509
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