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Macromolecular Protein Complexes III: Structure and Function: Subcellular Biochemistry, cartea 96

Editat de J. Robin Harris, Jon Marles-Wright
en Limba Engleză Paperback – 2 dec 2021
This book covers important topics such as the dynamic structure and function of the 26S proteasome, the DNA replication machine: structure and dynamic function and the structural organization and protein–protein interactions in the human adenovirus capsid, to mention but a few.
The 18 chapters included here, written by experts in their specific field, are at the forefront of scientific knowledge. The impressive integration of structural data from X-ray crystallography with that from cryo-electron microscopy is apparent throughout the book. In addition, functional aspects are also given a high priority.
Chapter 1 is available open access under a Creative Commons Attribution 4.0 International License via link.springer.com.
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Specificații

ISBN-13: 9783030589738
ISBN-10: 3030589730
Pagini: 577
Ilustrații: VIII, 577 p. 166 illus., 157 illus. in color.
Dimensiuni: 155 x 235 mm
Ediția:1st ed. 2021
Editura: Springer International Publishing
Colecția Springer
Seria Subcellular Biochemistry

Locul publicării:Cham, Switzerland

Cuprins

Chapter 1. Structure, Dynamics and Function of the 26S Proteasome.- Chapter 2. Factor VIII and Factor V Membrane Bound Complexes.- Chapter 3. An Overview of DPS: Dual Acting Nanovehicles in Prokaryotes with DNA Binding and Ferroxidation Properties.- Chapter 4. Structure and Function of the Separase-Securin Complex.- Chapter 5. The DNA Replication Machine: Structure and Dynamic Function.- Chapter 6. Recent Progress in Structural Studies on the GT-C Superfamily of Protein Glycosyltransferases.- Chapter 7. How Structures of Complement Complexes Guide Therapeutic Design.- Chapter 8. Architecture and Assembly of the Bacterial Flagellar Motor Complex.- Chapter 9. Cellulosomes: Highly Efficient Cellulolytic Complexes.- Chapter 10. Leucine Dehydrogenase: Structure and Thermostability.- Chapter 11. Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3.- Chapter 12. The SF3b Complex Is an Integral Component of the Spliceosome and Targeted byNatural Product-based Inhibitors.- Chapter 13. Interaction Networks of Ribosomal Expansion Segments in Kinetoplastids.- Chapter 14. Hepatitis B Core Protein Capsids.- Chapter 15. Fibrinogen and Fibrin.- Chapter 16. Structural Organization and Protein-protein Interactions in Human Adenovirus Capsid.- Chapter 17. A Structural Perspective on Gene Repression by Polycomb Repressive Complex 2.- Chapter 18. Assembly and Function of the Anthrax Toxin Protein Translocation Complex.

Notă biografică

Dr J. Robin Harris is a retired biochemist with specialism in macromolecular electron microscopy, now based in the UK.  He is the long-standing Series Editor of Subcellular Biochemistry. He is an Honorary Professor of the University of Mainz. Dr Jon Marles-Wright is a Senior Lecturer in the School of Natural and Environmental Sciences at Newcastle University. He has broad interest and experience in biomolecular X-ray  crystallography and cryoelectron microscopy.

Textul de pe ultima copertă

This book covers important topics such as the dynamic structure and function of the 26S proteasome, the DNA replication machine: structure and dynamic function and the structural organization and protein–protein interactions in the human adenovirus capsid, to mention but a few. The 18 chapters included here, written by experts in their specific field, are at the forefront of scientific knowledge. The impressive integration of structural data from X-ray crystallography with that from cryo-electron microscopy is apparent throughout the book. In addition, functional aspects are also given a high priority.
Chapter 1 is available open access under a Creative Commons Attribution 4.0 International License vialink.springer.com.

Caracteristici

Broadens understanding of the biochemistry of a variety of macromolecular protein complexes Addresses both structural and functional aspects Is richly illustrated with molecular models derived from X-ray diffraction and Cryo-EM data