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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Sample Preparation Methods to Analyze DNA-Induced Structural Changes in Replication Protein A,neutron scattering (SAXS/SANS), when integrated with computational methods, can provide critical insights into the architectural changes associated with RPA’s different DNA-binding modes. The success of these methods, however, is highly contingent upon the purity, homogeneity, and stability of the s

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Detecting Posttranslational Modifications of Bacterial SSB Proteins,tro. Mass spectrometry analysis of SsbA identified Tyr82 as the phosphorylation site. Analyses of the resolved and predicted crystal structures of SSB proteins from ., ., and . revealed that the Tyr phosphorylation site occupies similar positions in all three structures. Our results indicate that ty

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Book 2012d 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

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Ammonium Sulfate Co-precipitation of SSB and Interacting Proteins, are mediated by the essential and conserved amphipathic C-terminus (SSB-Ct). SSB plays a critical role in localizing and stimulating the activity of a wide variety of DNA-processing proteins. The interaction partners have been identified and studied using a variety of methods, one of which, ammonium sulfate co-precipitation, is described here.

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Methods in Molecular Biologyhttp://image.papertrans.cn/s/image/867862.jpg

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https://doi.org/10.1007/978-1-62703-032-8DNA-binding proteins; SSB proteins; genome maintenance enzymes; heterologous protein complexes; ssDNA; Pr

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978-1-4939-6251-8Springer Science+Business Media, LLC 2012

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