Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes (Q48233551)

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scientific article published in January 2010

Language	Label	Description	Also known as
English	Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes	scientific article published in January 2010

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

author name string

Dmitrii E Makarov

1

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

language of work or name

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publication date

1 January 2010

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

Journal of Chemical Physics

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

132

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

3

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

035104

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

Excluded volume in the configurational distribution of a strongly-denatured protein

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Are denatured proteins ever random coils?

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Coil-globule transition in the denatured state of a small protein

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Using fluorescence correlation spectroscopy to study conformational changes in denatured proteins

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Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR Measurements

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Identifiers

10.1063/1.3284509

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/20095754

ResearchGate publication ID

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