Fluorescence characterization of denatured proteins.

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Fluorescence characterization of denatured proteins. Abstract Text:

Characterization of unfolded states, while critical to a complete understanding of protein folding, is inherently difficult due to structural heterogeneity and dynamic interchange between states. The growing body of work focusing on single molecule fluorescence techniques for the study of protein folding, also highlights their potential for studies of unfolded proteins. These methods can obtain conformational information about individual subpopulations of molecules in an ensemble, and measure dynamics without the need for synchronization. The studies highlighted here demonstrate the promise of these techniques for obtaining novel information about unfolded states in vitro and in more physiologically relevant milieu.

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Fluorescence characterization of denatured proteins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Current opinion in structural biology

VOLUME: 18

Page Numbers: 516-24

Journal Abbreviation: Curr. Opin. Struct. Biol.

ISSN: 0959-440X

DAY: 12

MONTH: 08

YEAR: 2008

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LANGUAGE: eng

NlmUniqueID: 9107784

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Grant and Affiliation Information for Fluorescence characterization of denatured proteins.

AFFILIATION: School of Applied and Engineering Physics, Cornell University, Ithaca, NY 14853, USA.

Country: England

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MEDLINETA: Curr Opin Struct Biol

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