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Titlebook: Chromosome Architecture; Methods and Protocol Mark C. Leake Book 2022Latest edition The Editor(s) (if applicable) and The Author(s), under

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發(fā)表于 2025-3-21 17:06:48 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Chromosome Architecture
副標(biāo)題Methods and Protocol
編輯Mark C. Leake
視頻videohttp://file.papertrans.cn/227/226342/226342.mp4
概述Includes cutting-edge techniques.Provides step-by-step detail essential for reproducible results.Contains key implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Chromosome Architecture; Methods and Protocol Mark C. Leake Book 2022Latest edition The Editor(s) (if applicable) and The Author(s), under
描述This detailed new edition collects cutting-edge laboratory protocols, techniques, and applications in use by some of the leading international experts in the broad field of chromosome architecture. The book emphasizes the increasing physiological relevance of chromosome architecture investigation, manifest both through application of more complex bottom-up assays .in vitro. as well as through maintaining the native physiological context through the investigation of living, functional cells. In addition, the chapters reflect the dramatic improvement in the length scale of precision by utilizing single-molecule approaches, both for imaging the DNA content of chromosome and proteins that bind to DNA as well as using methods that can controllably manipulate single DNA molecules, and the use of advanced computational methods and mathematical analysis is also featured. Written for the highly successful .Methods in Molecular Biology. series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.?.Authoritative and up-to-date,
出版日期Book 2022Latest edition
關(guān)鍵詞Living cells; Length scale; Single-molecule approaches; DNA content; Protein binding
版次2
doihttps://doi.org/10.1007/978-1-0716-2221-6
isbn_softcover978-1-0716-2223-0
isbn_ebook978-1-0716-2221-6Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
The information of publication is updating

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發(fā)表于 2025-3-21 20:56:46 | 只看該作者
Single-Molecule Narrow-Field Microscopy of Protein-DNA Binding Dynamics in Glucose Signal Transductused in bacteria. Here, we describe how these methods can be extended to larger eukaryotic, yeast cells, which contain subcellular compartments. We describe how to obtain single-molecule microscopy data but also how to analyze these data to track and obtain the stoichiometry of molecular complexes d
板凳
發(fā)表于 2025-3-22 01:23:18 | 只看該作者
Convolutional Neural Networks for Classifying Chromatin Morphology in Live-Cell Imaging,in machine learning have enabled researchers to automatically classify chromatin morphology in fluorescence microscopy images. In this protocol, we develop user-friendly tools to perform this task. We provide an open-source annotation tool, and a cloud-based computational framework to train and util
地板
發(fā)表于 2025-3-22 07:44:59 | 只看該作者
Fluorescence Recovery After Photobleaching (FRAP) to Study Dynamics of the Structural Maintenance oescently tagged MukBEF forms distinct spots (or “foci”) composed of molecular assemblies in the cell, where it is thought to carry out most of its chromosome-associated activities. Here, we outline the technique of fluorescence recovery after photobleaching (FRAP) as a method to study the properties
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發(fā)表于 2025-3-22 11:27:49 | 只看該作者
Atomic Force Microscopy of DNA and DNA-Protein Interactions,ications, one of its key advantages is its ability to visualize the substructure of single molecules and molecular complexes in an aqueous environment. Here, we describe the application of AFM to determine the secondary and tertiary structure of surface-bound DNA, and its interactions with proteins.
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Atomistic Molecular Dynamics Simulations of DNA in Complex 3D Arrangements for Comparison with Loweng detail at a resolution where experimental techniques cannot arrive. Molecular dynamics (MD) simulations of mechanically distorted DNA caused by agents like supercoiling and protein binding are computationally challenging due to the large size of the associated systems and timescales. However, now
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發(fā)表于 2025-3-23 09:29:12 | 只看該作者
DNA-Protein Interactions Studied Directly Using iSCAT Imaging of GNP-Tagged Proteins,eatures are facile to include in a study. For single-molecule imaging this can be more difficult, because the constraints of the assay limit the variety of adducts that can be used. Surface-immobilized DNA provides an ideal compromise, and the use of interferometric scattering microscopy allows for
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