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Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_743074214

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

About this item

Full title

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Publisher

Washington, DC: American Association for the Advancement of Science

Journal title

Science (American Association for the Advancement of Science), 2003-10, Vol.302 (5643), p.262-266

Language

English

Formats

Publication information

Publisher

Washington, DC: American Association for the Advancement of Science

More information

Scope and Contents

Contents

Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe...

Alternative Titles

Full title

Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_743074214

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_743074214

Other Identifiers

ISSN

0036-8075

E-ISSN

1095-9203

DOI

10.1126/science.1086911

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