DNA Helicases and DNA Motor Proteins, Maria Spies

Автор: David B. Lombard
Название: Biochemistry and Genetics of Recq-Helicases
ISBN: 1461355370 ISBN-13(EAN): 9781461355373
Издательство: Springer
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Цена: 93160.00 T
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Описание: Biochemistry And Genetics of RecQ-Helicases provides a background into the role of helicases in general and RecQ helicases specifically in DNA repair. The RecQ-family helicases are a group of helicases which have important roles in the maintenance of genomic stability in many organisms.

Автор: Ulrich Huebscher
Название: Proteins Involved in DNA Replication
ISBN: 1468487329 ISBN-13(EAN): 9781468487329
Издательство: Springer
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Цена: 93160.00 T
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Автор: James L. Keck
Название: Single-Stranded DNA Binding Proteins
ISBN: 1493962515 ISBN-13(EAN): 9781493962518
Издательство: Springer
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Цена: 111790.00 T
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Описание: This Methods in Molecular Biology (TM) book offers techniques for examining fundamental properties of SSBs and for exploiting the biochemical functions of SSBs as in vitro and in vivo reagents. Includes materials lists, protocols, troubleshooting tips and more.

Автор: Yogambigai Velmurugu
Название: Dynamics and Mechanism of DNA-Bending Proteins in Binding Site Recognition
ISBN: 3319451286 ISBN-13(EAN): 9783319451282
Издательство: Springer
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Цена: 111790.00 T
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Описание: 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.