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Titlebook: Glycobiophysics; Yoshiki Yamaguchi,Koichi Kato Book 2018 Springer Nature Singapore Pte Ltd. 2018 Glycoscience.Glycochemistry.Structural Gl

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發(fā)表于 2025-3-21 17:52:32 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Glycobiophysics
編輯Yoshiki Yamaguchi,Koichi Kato
視頻videohttp://file.papertrans.cn/388/387086/387086.mp4
概述Discusses new knowledge gained through a multidisciplinary biophysical approach.Describes emerging biophysical techniques in detail.Discusses up-to-date applications in glycobiophysics
叢書名稱Advances in Experimental Medicine and Biology
圖書封面Titlebook: Glycobiophysics;  Yoshiki Yamaguchi,Koichi Kato Book 2018 Springer Nature Singapore Pte Ltd. 2018 Glycoscience.Glycochemistry.Structural Gl
描述.This book presents state of the art biophysical approaches to issues in glycobiology that have cutting-edge applications. Despite the importance of glycosylation, the complexity, heterogeneity, and flexibility of the glycans have inhibited their study. Each chapter in this book explains very recent significant advances in biophysical approaches through the use of techniques such as NMR spectroscopy, mass spectrometry, single-molecule imaging, X-ray crystallography, high-speed atomic force microscopy, and computational simulation and their integrative application.?Concrete examples are provided of the value of these techniques in addressing key problems in the field. In addition, significant functional glycobiological issues are considered. For example, glycolipids can form dynamic clusters on cell membranes and provide platforms for molecules involved in cell recognition and subsequent signal transduction. The detailed delineation of these molecular systems is discussed, revealing their structural complexity and ability to assemble transiently.?This timely book will be of value for graduate students and postdocs interested in frontier topics in glycoscience and also for senior bio
出版日期Book 2018
關(guān)鍵詞Glycoscience; Glycochemistry; Structural Glycobiology; Glycosylation; Glycolipids
版次1
doihttps://doi.org/10.1007/978-981-13-2158-0
isbn_ebook978-981-13-2158-0Series ISSN 0065-2598 Series E-ISSN 2214-8019
issn_series 0065-2598
copyrightSpringer Nature Singapore Pte Ltd. 2018
The information of publication is updating

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發(fā)表于 2025-3-21 23:33:18 | 只看該作者
Biophysical Analyses for Probing Glycan-Protein Interactions,sis, 3D structural analysis, and molecular dynamics simulation. Our increasing knowledge and understanding of lectin-glycan interactions will hopefully lead to the design of glyco-based medicines and vaccines.
板凳
發(fā)表于 2025-3-22 02:18:36 | 只看該作者
Structural Basis of Protein Asn-Glycosylation by Oligosaccharyltransferases,LO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions
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發(fā)表于 2025-3-22 08:09:36 | 只看該作者
Structure and Dynamics of Immunoglobulin G Glycoproteins,ms underlying the glycofunctions of this interacting system. The .-glycans of IgG and FcγR mediate their interactions by either strengthening or weakening the affinity on the basis of their glycoforms. Moreover, the .-glycosylation of IgG-Fc is a prerequisite to maintain the integrity of the quatern
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Controlling im Pflegemanagement,sis, 3D structural analysis, and molecular dynamics simulation. Our increasing knowledge and understanding of lectin-glycan interactions will hopefully lead to the design of glyco-based medicines and vaccines.
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發(fā)表于 2025-3-22 23:06:02 | 只看該作者
https://doi.org/10.1007/978-3-211-89865-9LO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions
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Einfache und aufl?sbare Gruppen*rms remained elusive for years because initial attempts to solve their structures used tools developed for eukaryotic-like systems, which we now know are not suitable for this noncanonical glycosylation pattern. This chapter summarizes the methods used to solve the chlorovirus complex glycan structu
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