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Single-molecule fluorescence spectro...
~
Cohen, Sharona.
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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 protein/ by Sharona Cohen.
Author:
Cohen, Sharona.
Published:
Cham :Springer International Publishing : : 2016.,
Description:
xiii, 59 p. :ill., digital ;24 cm.
[NT 15003449]:
Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans.
Contained By:
Springer eBooks
Subject:
Proteins - Spectra. -
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:
687705
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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Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans.
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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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Chemistry and Materials Science (Springer-11644)
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Opac note
Attachments
W9276074
電子資源
11.線上閱覽_V
電子書
EB QP551 .C678 2016
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