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Titlebook: DNA-Protein Interactions; Principles and Proto Benoît Leblanc,Tom Moss Book 2009Latest edition Humana Press 2009 Chromatin immunoprecipitat

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书目名称DNA-Protein Interactions
副标题Principles and Proto
编辑Benoît Leblanc,Tom Moss
视频video
概述Covers cutting edge techniques in chromatin studies, such as Nucleosome Mapping, Chromatin Immunoprecipitation and ChIP-on-chip.Contains many protocols for large scale analysis of genome-protein inter
丛书名称Methods in Molecular Biology
图书封面Titlebook: DNA-Protein Interactions; Principles and Proto Benoît Leblanc,Tom Moss Book 2009Latest edition Humana Press 2009 Chromatin immunoprecipitat
描述.Gene expression can mean the difference between a functional and non-functional genome, between health and disease, and with the development of transgenic crops, the difference between survival and starvation. In .DNA-Protein Interactions: Principles and Protocols, Third Edition., this vital subject is brought up to date with protocols exploring the most cutting-edge developments in the field, including .in vivo. and genome-wide interaction techniques. Addressing topics such as chromatin immunoprecipitation, topological studies, photocrosslinking, FRET and imaging techniques, the volume fully updates and expands upon the successful previous editions. Written in the convenient and informative .Methods in Molecular Biology™. series format, chapters include introductions to their respective subjects, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls....Comprehensive and authoritative, .DNA-Protein Interactions: Principles and Protocols, Third Edition. serves as an ideal guide for all those exploring this dynamic, essential, and increasingly affordable area of research..
出版日期Book 2009Latest edition
关键词Chromatin immunoprecipitation; DNA; Genome-wide techniques; In vivo techniques; Microarray; PCR; Photocros
版次3
doihttps://doi.org/10.1007/978-1-60327-015-1
isbn_softcover978-1-61737-875-1
isbn_ebook978-1-60327-015-1Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 2009
The information of publication is updating

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DNase I Footprinting,using bulky nucleases such as DNAse I. The DNAse I footprinting method was developed to make use of this phenomenon in the study of DNA–protein interactions; it consists in comparing the pattern of fragments produced by the partial digestion of DNA in the absence of a protein to that produced by par
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Exonuclease III Footprinting on Immobilized DNA Templates, protects it from degradation by an enzyme or chemical reagent..Exonuclease III is a suitable probe to analyze the boundaries of a protein when it is necessary to eliminate any excess unbound DNA from the reaction to avoid background problems. In combination with biotin-labeled DNA that is bound to
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Hydroxyl Radical Footprinting of Protein-DNA Complexes,cts between a protein and its cognate DNA and details of the complex structure. We describe several methods to prepare DNA templates for footprinting and ways to avoid many of the pitfalls associated with the use of hydroxyl radical footprinting. In addition, we describe in detail one example of the
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Uranyl Photofootprinting,elength ultraviolet light (. = 300–420 nm), uranyl ions bound to backbone phosphates oxidize proximal sugars and induce nucleic acid backbone cleavage. Thus the uranyl(VI) ion functions as a very specific and efficient photochemical probe for identifying ligand(protein)-phosphate contacts in nucleic
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Identification of Protein/DNA Contacts with Dimethyl Sulfate: Methylation Protection and Methylatiol probes, such as dimethyl sulfate, have been used to obtain information on these sites of interaction. Protection and interference patterns frequently correspond to highly conserved positions within binding sites and are often specific for a given transcription factor or family of factors. The meth
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Identification of Nucleic Acid High-Affinity Binding Sequences of Proteins by SELEX,rtitioning assay. Here, a histidine-tagged protein is allowed to interact with a pool of nucleic acids and the protein–nucleic acid complexes formed are retained on a Ni-NTA matrix. Nucleic acids with a low level of recognition by the protein are washed away. The pool of recovered nucleic acids is a
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