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Titlebook: Enzyme-Mediated Ligation Methods; Timo Nuijens,Marcel Schmidt Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019

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發(fā)表于 2025-3-21 19:47:00 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Enzyme-Mediated Ligation Methods
編輯Timo Nuijens,Marcel Schmidt
視頻videohttp://file.papertrans.cn/314/313103/313103.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: Enzyme-Mediated Ligation Methods;  Timo Nuijens,Marcel Schmidt Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019
描述.This volume discusses different enzyme-catalyzed ligation methodologies for a variety of different chemical transformations. This book wants readers to view enzymes as a powerful tool in both academic and industrial research. Chapters in this book cover topics such as sortase A-mediated generation of site-specifically conjugated antibody-drug conjugates; omniligase-catalyzed inter- and intramolecular ligation; ligation catalyzed by microbial transglutaminase; peptide cyclization mediated by cyanobactin macrocyclases, butelase 1 and sortase A; using BioID as a tool for protein proximity labeling in living cells; and inducible, selective labeling of proteins via enzymatic oxidation of tyrosine. Written in the highly successful .Methods in Molecular Biology. series format, 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..Cutting-edge and thorough, .Enzyme-Mediated Ligation Methods. is a valuable resource for students and scientists from different disciplines who are interested in using enzymatic strategies to answer
出版日期Book 2019
關(guān)鍵詞biotherapeutics; phosphopantheinyl transferase; Glutathione-S-Transferase; Peptide Coupling; cyclization
版次1
doihttps://doi.org/10.1007/978-1-4939-9546-2
isbn_softcover978-1-4939-9548-6
isbn_ebook978-1-4939-9546-2Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2019
The information of publication is updating

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Chemoenzymatic Synthesis of Linear- and Head-to-Tail Cyclic Peptides Using Omniligase-1,peptides. Reactions are irreversible and proceed with unprotected peptides (μM–mM?concentration) in aqueous solution at slightly basic pH. Due to its high catalytic efficiency, only very low molar equivalents of omniligase-1 are required. In this chapter, a chemoenzymatic peptide synthesis (CEPS) ap
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Site-Specific Labeling of Proteins Using the Formylglycine-Generating Enzyme (FGE),directly from nature of introducing a unique amino acid into the larger context of a protein. Formylglycine (fGly) is a crucial component of the active site of sulfatases, where it directly participates in the breakdown of sulfate ester substrates. In the context of bioconjugation this aldehyde cont
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Butelase 1-Mediated Ligation of Peptides and Proteins,Asx) ligase activity and is virtually devoid of protease activity. Butelase 1 recognizes specifically a .-terminal Asx-containing tripeptide motif, Asx-His-Val, to form an Asx-Xaa peptide bond (Xaa?=?any amino acid), either intramolecularly or intermolecularly, resulting in cyclic peptides or site-s
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Trypsiligase-Catalyzed Peptide and Protein Ligation,sents a major challenge to protein chemists. Chemical labeling methods often target multiple positions within a protein and therefore suffer from a lack of specificity. Enzymatic protein modification is an attractive alternative due to the inherent regioselectivity and stereoselectivity of enzymes.
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SpyLigase-Catalyzed Modification of Antibodies,ifferent cell populations as well as for tracking intracellular pathways. In recent years, antibody–drug conjugates (ADCs) have emerged as promising therapeutics to treat cancer and have moved into the focus of interest of the pharmaceutical industry. Here we describe a conjugation method for the ge
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