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Titlebook: Non-Ribosomal Peptide Biosynthesis and Engineering; Methods and Protocol Michael Burkart,Fumihiro Ishikawa Book 2023 The Editor(s) (if appl

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書目名稱Non-Ribosomal Peptide Biosynthesis and Engineering
副標(biāo)題Methods and Protocol
編輯Michael Burkart,Fumihiro Ishikawa
視頻videohttp://file.papertrans.cn/668/667020/667020.mp4
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
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Non-Ribosomal Peptide Biosynthesis and Engineering; Methods and Protocol Michael Burkart,Fumihiro Ishikawa Book 2023 The Editor(s) (if appl
描述.This volume provides new technologies on NRPSs and related carrier protein dependent synthases, including polyketide synthases (PKS) and fatty acid synthases (FAS). Chapters detail enzymology, structural biology, proteopromics, chemical biology, natural product chemistry, and bioinformatics. Written in the format of the highly successful?.Methods in Molecular Biology?.series, each chapter includes an introduction to the topic, lists necessary materials and methods, includes tips on troubleshooting and known pitfalls, and step-by-step, readily reproducible protocols..?Authoritative and cutting-edge, .Non-Ribosomal Peptide Biosynthesis and Engineering: Methods and Protocols .aims to feature methods that will be beneficial to new researchers, and those wanting to adopt new methodologies into their research..
出版日期Book 2023
關(guān)鍵詞Non-ribosomal peptide synthetases (NRPSs); Peptide natural products; Biosynthetic enzymes; Bioinformati
版次1
doihttps://doi.org/10.1007/978-1-0716-3214-7
isbn_softcover978-1-0716-3216-1
isbn_ebook978-1-0716-3214-7Series 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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Unraveling Structural Information of Multi-Domain Nonribosomal Peptide Synthetases by Using Photo-Crdy the communication (COM) domains, a special pair of docking domains of unknown structure between two interacting subunits of one NRPS system, this cross-linking approach was also found to be useful to interrogate the spatial proximity of domains that are not connected on the level of the primary s
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Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonancental readouts necessary to assess the integrity of the sample and maintain loading on CPs. Our approach provides a basis to conduct subsequent NMR experiments and obtain kinetic, thermodynamic, dynamic, and structural parameters of substrate-loaded CPs alone or in the presence of other domains.
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