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Titlebook: Single-Stranded DNA Binding Proteins; Methods and Protocol James L. Keck Book 2012 Springer Science+Business Media, LLC 2012 DNA-binding pr

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发表于 2025-3-21 19:41:27 | 显示全部楼层 |阅读模式
书目名称Single-Stranded DNA Binding Proteins
副标题Methods and Protocol
编辑James L. Keck
视频video
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts.Includes supplementary materia
丛书名称Methods in Molecular Biology
图书封面Titlebook: Single-Stranded DNA Binding Proteins; Methods and Protocol James L. Keck Book 2012 Springer Science+Business Media, LLC 2012 DNA-binding pr
描述.The genomes of cellular organisms are organized as double-stranded DNA, a structure that must be unwound to provide DNA replication, recombination, and repair machinery access to genomic information.  However, DNA unwinding comes with inherent risks to genome stability.  To help mediate these risks, bacterial, archael, and eukaryotic cells have evolved protective ssDNA-binding proteins (SSBs) that bind ssDNA with high affinity and specificity.  SSBs also aid genome metabolic processes through direct interactions with key proteins in genome maintenance enzymes.  .Single-Stranded DNA Binding Proteins: Methods and Protocols. assembles methods developed for examining the fundamental properties of SSBs and for exploiting the biochemical functions of SSBs for their use as in vitro and in vivo reagents. Clearly and concisely organized, the volume opens with an introduction to the structures and functions of SSBs, followed protocols for studying SSB/DNA complexes, methods for studying SSB/heterologous protein complexes, protocols for interrogating post-translational modifications of SSBs, and concludes with uses of fluorescently-labeled SSBs for in vitro and in vivo studies of genome main
出版日期Book 2012
关键词DNA-binding proteins; SSB proteins; genome maintenance enzymes; heterologous protein complexes; ssDNA; Pr
版次1
doihttps://doi.org/10.1007/978-1-62703-032-8
isbn_softcover978-1-4939-6251-8
isbn_ebook978-1-62703-032-8Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC 2012
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Book 2012nd repair machinery access to genomic information.  However, DNA unwinding comes with inherent risks to genome stability.  To help mediate these risks, bacterial, archael, and eukaryotic cells have evolved protective ssDNA-binding proteins (SSBs) that bind ssDNA with high affinity and specificity. 
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Structural Studies of SSB Interaction with RecO,d a high-resolution structure of RecO complex with C-terminal tail of SSB (SSB-Ct). The structure revealed a key role of hydrophobic interactions between two proteins and suggests the mechanism of RecO recruitment to DNA during homologous recombination and strand annealing.
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Analyzing Interactions Between SSB and Proteins by the Use of Fluorescence Anisotropy,SSB peptide alone. Thus the tumbling of the complexes in solution is slower, and the fluorescence anisotropy (FA) signal would be increased, indicating the binding. Based on the FA binding curve, the apparent dissociation constant (..) of the binding reaction can also be calculated.
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