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Single-molecule fluorescence spectro...

Cohen, Sharona.

Single-molecule fluorescence spectroscopy of the folding of a repeat protein

Record Type:	Electronic resources : Monograph/item
Title/Author:	Single-molecule fluorescence spectroscopy of the folding of a repeat proteinby Sharona Cohen.
Author:	Cohen, Sharona.
Published:	Cham :Springer International Publishing :2016.
Description:	xiii, 59 p. :ill., digital ;24 cm.
Contained By:	Springer eBooks
Subject:	ProteinsSpectra.
Online resource:	http://dx.doi.org/10.1007/978-3-319-09558-5
ISBN:	9783319095585$q(electronic bk.)

Single-molecule fluorescence spectroscopy of the folding of a repeat protein
Cohen, Sharona.

Single-molecule fluorescence spectroscopy of the folding of a repeat protein[electronic resource] /by Sharona Cohen. - Cham :Springer International Publishing :2016. - xiii, 59 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..

Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans.

In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field.

ISBN: 9783319095585$q(electronic bk.)

Standard No.: 10.1007/978-3-319-09558-5doiSubjects--Topical Terms:

224961
Proteins
--Spectra.

LC Class. No.: QP551

Dewey Class. No.: 572.6

Single-molecule fluorescence spectroscopy of the folding of a repeat protein
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505 0 $a Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans.
520 $a In this thesis single-molecule fluorescence resonance energy transfer (FRET) spectroscopy was used to study the folding of a protein that belongs to the large and important family of repeat proteins. Cohen shows that the dynamics of the expanded conformations is likely to be very fast, suggesting a spring-like motion of the whole chain. The findings shed new light on the elasticity of structure in repeat proteins, which is related to their function in binding multiple and disparate partners. This concise research summary provides useful insights for students beginning a PhD in this or a related area, and researchers entering this field.
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