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Single-molecule fluorescence spectro...

Cohen, Sharona.

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

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Single-molecule fluorescence spectroscopy of the folding of a repeat protein/ by Sharona Cohen.
作者:	Cohen, Sharona.
出版者:	Cham :Springer International Publishing : : 2016.,
面頁冊數:	xiii, 59 p. :ill., digital ; : 24 cm.;
Contained By:	Springer eBooks
標題:	Proteins - Spectra. -
電子資源:	http://dx.doi.org/10.1007/978-3-319-09558-5
ISBN:	9783319095585

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

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

891163
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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245 1 0 $a Single-molecule fluorescence spectroscopy of the folding of a repeat protein $h [electronic resource] / $c by Sharona Cohen.
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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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