大葉大學圖書館 |

登入

回首頁

Single-molecule fluorescence spectro...

Cohen, Sharona.

Single-molecule fluorescence spectroscopy of the folding of a repeat protein[electronic resource] /

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
杜威分類號:	572.6
書名/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.
標題:	Fluorescence spectroscopy.
標題:	Protein folding.
標題:	Chemistry.
標題:	Bioorganic Chemistry.
標題:	Spectroscopy/Spectrometry.
標題:	Biophysics and Biological Physics.
ISBN:	9783319095585
ISBN:	9783319095578
內容註:	Abstract -- Introduction -- Methods -- Results -- Discussion -- Summary and Future Plans.
摘要、提要註:	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.
電子資源:	http://dx.doi.org/10.1007/978-3-319-09558-5

Single-molecule fluorescence spectroscopy of the folding of a repeat protein[electronic resource] /
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:

468884
Proteins
--Spectra.

LC Class. No.: QP551

Dewey Class. No.: 572.6

Single-molecule fluorescence spectroscopy of the folding of a repeat protein[electronic resource] /
LDR:01768nam a2200337 a 4500 001 454616
003 DE-He213
005 20160725121134.0
006 m d
007 cr nn 008maaau
008 161227s2016 gw s 0 eng d
020 $a 9783319095585 $q (electronic bk.)
020 $a 9783319095578 $q (paper)
024 7 $a 10.1007/978-3-319-09558-5 $2 doi
035 $a 978-3-319-09558-5
040 $a GP $c GP
041 0 $a eng
050 4 $a QP551
072 7 $a PSB $2 bicssc
072 7 $a SCI013040 $2 bisacsh
072 7 $a SCI007000 $2 bisacsh
082 0 4 $a 572.6 $2 23
090 $a QP551 $b .C678 2016
100 1 $a Cohen, Sharona. $3 652240
245 1 0 $a Single-molecule fluorescence spectroscopy of the folding of a repeat protein $h [electronic resource] / $c by Sharona Cohen.
260 $a Cham : $b Springer International Publishing : $b Imprint: Springer, $c 2016.
300 $a xiii, 59 p. : $b ill., digital ; $c 24 cm.
490 1 $a Springer theses, $x 2190-5053
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.
650 0 $a Proteins $x Spectra. $3 468884
650 0 $a Fluorescence spectroscopy. $3 428097
650 0 $a Protein folding. $3 445225
650 1 4 $a Chemistry. $3 182539
650 2 4 $a Bioorganic Chemistry. $3 463749
650 2 4 $a Spectroscopy/Spectrometry. $3 464483
650 2 4 $a Biophysics and Biological Physics. $3 464224
710 2 $a SpringerLink (Online service) $3 463450
773 0 $t Springer eBooks
830 0 $a Springer theses. $3 463746
856 4 0 $u http://dx.doi.org/10.1007/978-3-319-09558-5
950 $a Chemistry and Materials Science (Springer-11644)

筆 0 讀者評論

多媒體

多媒體檔案
http://dx.doi.org/10.1007/978-3-319-09558-5

評論

新增評論分享你的心得

Export

取書館別