語系:
繁體中文
English
說明(常見問題)
登入
回首頁
切換:
標籤
|
MARC模式
|
ISBD
Dynamics and mechanism of DNA-bendin...
~
Velmurugu, Yogambigai.
Dynamics and mechanism of DNA-bending proteins in binding site recognition
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Dynamics and mechanism of DNA-bending proteins in binding site recognition/ by Yogambigai Velmurugu.
作者:
Velmurugu, Yogambigai.
出版者:
Cham :Springer International Publishing : : 2017.,
面頁冊數:
xxi, 199 p. :ill., digital ; : 24 cm.;
Contained By:
Springer eBooks
標題:
DNA-binding proteins. -
電子資源:
http://dx.doi.org/10.1007/978-3-319-45129-9
ISBN:
9783319451299
Dynamics and mechanism of DNA-bending proteins in binding site recognition
Velmurugu, Yogambigai.
Dynamics and mechanism of DNA-bending proteins in binding site recognition
[electronic resource] /by Yogambigai Velmurugu. - Cham :Springer International Publishing :2017. - xxi, 199 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..
Introduction -- Methods -- Integration Host Factor (IHF)-DNA interaction -- Lesion Recognition by Xeroderma Pigmentosum C (XPC) Protein -- DNA Mismatch Repair.
Using a novel approach that combines high temporal resolution of the laser T-jump technique with unique sets of fluorescent probes, this study unveils previously unresolved DNA dynamics during search and recognition by an architectural DNA bending protein and two DNA damage recognition proteins. Many cellular processes involve special proteins that bind to specific DNA sites with high affinity. How these proteins recognize their sites while rapidly searching amidst ~3 billion nonspecific sites in genomic DNA remains an outstanding puzzle. Structural studies show that proteins severely deform DNA at specific sites and indicate that DNA deformability is a key factor in site-specific recognition. However, the dynamics of DNA deformations have been difficult to capture, thus obscuring our understanding of recognition mechanisms. The experiments presented in this thesis uncover, for the first time, rapid (~100-500 microseconds) DNA unwinding/bending attributed to nonspecific interrogation, prior to slower (~5-50 milliseconds) DNA kinking/bending/nucleotide-flipping during recognition. These results help illuminate how a searching protein interrogates DNA deformability and eventually "stumbles" upon its target site. Submillisecond interrogation may promote preferential stalling of the rapidly scanning protein at cognate sites, thus enabling site-recognition. Such multi-step search-interrogation-recognition processes through dynamic conformational changes may well be common to the recognition mechanisms for diverse DNA-binding proteins.
ISBN: 9783319451299
Standard No.: 10.1007/978-3-319-45129-9doiSubjects--Topical Terms:
792141
DNA-binding proteins.
LC Class. No.: QP624.75.P74
Dewey Class. No.: 572.864
Dynamics and mechanism of DNA-bending proteins in binding site recognition
LDR
:02754nam a2200337 a 4500
001
957464
003
DE-He213
005
20161130135236.0
006
m d
007
cr nn 008maaau
008
201118s2017 gw s 0 eng d
020
$a
9783319451299
$q
(electronic bk.)
020
$a
9783319451282
$q
(paper)
024
7
$a
10.1007/978-3-319-45129-9
$2
doi
035
$a
978-3-319-45129-9
040
$a
GP
$c
GP
041
0
$a
eng
050
4
$a
QP624.75.P74
072
7
$a
PHVN
$2
bicssc
072
7
$a
PHVD
$2
bicssc
072
7
$a
SCI009000
$2
bisacsh
082
0 4
$a
572.864
$2
23
090
$a
QP624.75.P74
$b
V443 2017
100
1
$a
Velmurugu, Yogambigai.
$3
1249054
245
1 0
$a
Dynamics and mechanism of DNA-bending proteins in binding site recognition
$h
[electronic resource] /
$c
by Yogambigai Velmurugu.
260
$a
Cham :
$c
2017.
$b
Springer International Publishing :
$b
Imprint: Springer,
300
$a
xxi, 199 p. :
$b
ill., digital ;
$c
24 cm.
490
1
$a
Springer theses,
$x
2190-5053
505
0
$a
Introduction -- Methods -- Integration Host Factor (IHF)-DNA interaction -- Lesion Recognition by Xeroderma Pigmentosum C (XPC) Protein -- DNA Mismatch Repair.
520
$a
Using a novel approach that combines high temporal resolution of the laser T-jump technique with unique sets of fluorescent probes, this study unveils previously unresolved DNA dynamics during search and recognition by an architectural DNA bending protein and two DNA damage recognition proteins. Many cellular processes involve special proteins that bind to specific DNA sites with high affinity. How these proteins recognize their sites while rapidly searching amidst ~3 billion nonspecific sites in genomic DNA remains an outstanding puzzle. Structural studies show that proteins severely deform DNA at specific sites and indicate that DNA deformability is a key factor in site-specific recognition. However, the dynamics of DNA deformations have been difficult to capture, thus obscuring our understanding of recognition mechanisms. The experiments presented in this thesis uncover, for the first time, rapid (~100-500 microseconds) DNA unwinding/bending attributed to nonspecific interrogation, prior to slower (~5-50 milliseconds) DNA kinking/bending/nucleotide-flipping during recognition. These results help illuminate how a searching protein interrogates DNA deformability and eventually "stumbles" upon its target site. Submillisecond interrogation may promote preferential stalling of the rapidly scanning protein at cognate sites, thus enabling site-recognition. Such multi-step search-interrogation-recognition processes through dynamic conformational changes may well be common to the recognition mechanisms for diverse DNA-binding proteins.
650
0
$a
DNA-binding proteins.
$3
792141
650
1 4
$a
Physics.
$3
564049
650
2 4
$a
Biological and Medical Physics, Biophysics.
$3
1113305
650
2 4
$a
Spectroscopy and Microscopy.
$3
768852
650
2 4
$a
Protein-Ligand Interactions.
$3
882815
710
2
$a
SpringerLink (Online service)
$3
593884
773
0
$t
Springer eBooks
830
0
$a
Springer theses.
$3
831604
856
4 0
$u
http://dx.doi.org/10.1007/978-3-319-45129-9
950
$a
Physics and Astronomy (Springer-11651)
筆 0 讀者評論
多媒體
評論
新增評論
分享你的心得
Export
取書館別
處理中
...
變更密碼[密碼必須為2種組合(英文和數字)及長度為10碼以上]
登入