| Description |
1 online resource (xiii, 464 pages) : illustrations |
| Contents |
Cover -- Table Of Contents -- Preface -- Acknowledgements -- 1 Introduction -- 2 Solid State NMR Approach -- 2.1. CP-MAS and DD-MAS NMR -- 2.2. Quadrupolar Nuclei -- 3 Brief Outline of NMR Parameters -- 3.1. Chemical Shift -- 3.2. Relaxation Parameters -- 3.3. Dynamics-Dependent Suppression of Peaks -- 4 Multinuclear Approaches -- 4.1. [Sup(31)]P NMR -- 4.2.[Sup(2)]H NMR -- 4.3. [Sup(17)]O NMR -- 5 Experimental Strategies -- 5.1. Isotope Enrichment (Labeling) -- 5.2. Assignment of Peaks -- 5.3. Ultra-High Field and Ultra-High Speed MAS NMR -- 6 NMR Constraints for Determination of Secondary Structure -- 6.1. Orientational Constraint -- 6.2. Interatomic Distances -- 6.3. Torsion Angles -- 6.4. Conformation-Dependent Chemical Shifts -- 7 Dynamics -- 7.1. Fast Motions with Motional Frequency>10[Sup(6)] Hz -- 7.2. Intermediate or Slow Motions with Frequencies Between 10[Sup(6)] and 10[Sup(3)] Hz -- 7.3. Very Slow Motions with Frequency<10[Sup(3)] Hz -- 8 Hydrogen-Bonded Systems -- 8.1. Hydrogen Bond Shifts -- 8.2. [Sup(2)]H Quadrupolar Coupling Constant -- 9 Fibrous Proteins -- 9.1. Collagen Fibrils -- 9.2. Elastin -- 9.3. Cereal Proteins -- 9.4. Silk Fibroin -- 9.5. Keratins -- 9.6. Bacteriophage Coat Proteins -- 10 Polysaccharides -- 10.1. Distinction of Polymorphs -- 10.2. Network Structure, Dynamics, and Gelation Mechanism -- 11 Polypeptides as New Materials -- 11.1. Liquid-Crystalline Polypeptides -- 11.2. Blend System -- 12 Globular Proteins -- 12.1. (Almost) Complete Assignment of [Sup(13)]C NMR Spectra of Globular Proteins -- 12.2. 3D Structure: -Spectrin SH3 Domain -- 12.3. Ligand-Binding to Globular Protein -- 13 Membrane Proteins I: Dynamic Picture -- 13.1. Bacteriorhodopsin -- 13.2. Phoborhodopsin and Its Cognate Transducer -- 13.3. Diacylglycerol Kinase -- 14 Membrane Proteins II: 3D Structure -- 14.1. 3D Structure of Mechanically Oriented Membrane Proteins -- 14.2. Secondary Structure Based on Distance Constraints -- 15 Biologically Active Membrane-Associated Peptides -- 15.1. Channel-Forming Peptides -- 15.2. Antimicrobial Peptides -- 15.3. Opioid Peptides -- 15.4. Fusion Peptides -- 15.5. Membrane Model System -- 16 Amyloid and Related Biomolecules -- 16.1. Amyloid -Peptide (A) -- 16.2. Calcitonin -- Glossary -- Index -- Last Page |
| Summary |
Solid State NMR Spectroscopy for Biopolymers Principles and Applications by Hazime Saitô, Isao Ando and Akira Naito Unique and comprehensive coverage of solid state NMR, emphasising secondary structure and dynamics in relation to biological function. When considering the biological significance and industrial and medical applications of biopolymers, it is crucial to know details of their secondary structure, dynamics and assembly. The biopolymers include globular, membrane and fibrous proteins, polypeptides, nucleic acids, polysaccharides and lipids. Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. The major advantage of solid state NMR spectroscopy is that the resulting line widths can be manipulated experimentally and are not influenced by motional fluctuation of proteins under consideration as a whole. Solid State NMR Spectroscopy for Biopolymers: Principles and Applications provides a comprehensive account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR spectroscopy. Special efforts have been made towards the historical and chronological consequences of a variety of applications and the dynamic aspects of the biopolymer system. In particular, the authors emphasise how important it is to record the most simple DD-MAS (one pulse excitation with high power decoupling) as a mean of locating very flexible portions of membrane proteins and membrane associated peptides. The authors also demonstrate that dynamic features of membrane proteins with a timescale of fast (108 Hz) and intermediate (104 -105 Hz) fluctuation motions can be revealed easily by specific suppression of peaks. This book is an invaluable resource for biophysicists, biochemists and chemists, including NMR spectroscopists, structural biologists, and polymer scientists. The book provides an introduction suitable for graduate students as well as for research scientists, including those working in the pharmaceutical and chemical industries |
| Analysis |
chemie |
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chemistry |
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materialen |
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materials |
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fysische chemie |
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physical chemistry |
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polymeren |
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polymers |
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vaste stoffen |
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solids |
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fysica |
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physics |
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biomaterialen |
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biomaterials |
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materiaalkunde |
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materials science |
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Chemistry (General) |
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Chemie (algemeen) |
| Bibliography |
Includes bibliographical references and index |
| Notes |
English |
|
Print version record |
| In |
Springer e-books |
| Subject |
Biopolymers.
|
|
Nuclear magnetic resonance spectroscopy.
|
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Biopolymers
|
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Magnetic Resonance Spectroscopy
|
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SCIENCE -- Life Sciences -- Biochemistry.
|
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Nuclear magnetic resonance spectroscopy.
|
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Biopolymers.
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Chimie.
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Science des matériaux.
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Biopolymers
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Nuclear magnetic resonance spectroscopy
|
| Form |
Electronic book
|
| Author |
Ando, I. (Isao), 1941-
|
|
Naito, Akira, 1949-
|
| ISBN |
9781402043031 |
|
1402043031 |
|
1402043023 |
|
9781402043024 |
|
1280611510 |
|
9781280611513 |
|
6610611513 |
|
9786610611515 |
|
