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Titlebook: Dynamics and Mechanism of DNA-Bending Proteins in Binding Site Recognition; Yogambigai Velmurugu Book 2017 Springer International Publishi

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發(fā)表于 2025-3-21 16:37:21 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書(shū)目名稱Dynamics and Mechanism of DNA-Bending Proteins in Binding Site Recognition
編輯Yogambigai Velmurugu
視頻videohttp://file.papertrans.cn/284/283973/283973.mp4
概述Nominated as an outstanding PhD thesis by the University of Illinois at Chicago.Describes a novel approach combining the laser T-jump technique with unique sets of fluorescent probes to unveil previou
叢書(shū)名稱Springer Theses
圖書(shū)封面Titlebook: Dynamics and Mechanism of DNA-Bending Proteins in Binding Site Recognition;  Yogambigai Velmurugu Book 2017 Springer International Publishi
描述.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
出版日期Book 2017
關(guān)鍵詞Dynamics of protein DNA interactions; Laser temperature-jump spectroscopy; Protein-induced DNA bending
版次1
doihttps://doi.org/10.1007/978-3-319-45129-9
isbn_softcover978-3-319-83218-0
isbn_ebook978-3-319-45129-9Series ISSN 2190-5053 Series E-ISSN 2190-5061
issn_series 2190-5053
copyrightSpringer International Publishing AG, part of Springer Nature 2017
The information of publication is updating

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,Integration Host Factor (IHF)–DNA Interaction,here λ phage cleverly facilitates its . host’s protein IHF to infest its target, IHF also aids in chromosomal compaction as well as in the assembly of higher order nucleo-protein complexes necessary for replication initiation, some site-specific recombination and transcriptional regulation of certain genes [2, 3].
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DNA Mismatch Repair, also occur during genetic recombination or chemical modifications due to metabolic processes and environmental factors such as various types of ionizing radiation. The cells have evolved a complex network of repair pathway called mismatch repair pathway (MMR) to identify and correct the mistakes that escape DNA polymerase proofreading.
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Reflections on the Philosophy of Languagedesignated functions, proteins must first recognize and bind specifically to their target site on DNA. The study of the dynamics of protein–DNA interactions aimed at unraveling the mechanisms of binding-site recognition is a fascinating research field in biophysics and the central focus of this dissertation.
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Reflections on the Philosophy of Languagehere λ phage cleverly facilitates its . host’s protein IHF to infest its target, IHF also aids in chromosomal compaction as well as in the assembly of higher order nucleo-protein complexes necessary for replication initiation, some site-specific recombination and transcriptional regulation of certain genes [2, 3].
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Reflections on the Philosophy of Languagepic probe attached to the biomolecule. This time-resolved spectroscopy enables us to follow the conformational dynamics of the biomolecules over an enormous time-window from few nanoseconds to several milliseconds.
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