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Solid state NMR spectroscopy for biopolymers : principles and applications
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...
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| Auteurs principaux : | , , |
|---|---|
| Format : | Livre |
| Langue : | anglais |
| Titre complet : | Solid state NMR spectroscopy for biopolymers : principles and applications / by Hazime Saitô, Isao Ando, Akira Naito |
| Édition : | 1st ed. 2006. |
| Publié : |
Dordrecht :
Springer Netherlands
, [20..] Cham : Springer Nature |
| Accès en ligne : |
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| Contenu : | Part I: Principles: Solid state NMR approach: CP-MAS and DD-MAS NMR. Quadrupolar nuclei. Brief outline of NMR parameters: Chemical shifts. Relaxation parameters. Dynamics-dependent suppression of peaks. Multinuclear approaches: 31P NMR. 2H NMR. 17O NMR. Experimental strategies: Isotope enrichment (labeling). Assignment of peaks. Ultra high-field and ultra high-speed MAS NMR spectroscopy. NMR constraints for structural determination: Orientational constraint. Interatomic distance. Torsion angles. Conformation-dependent 13C chemical shifts. Dynamics: Fast motions with motional frequency >106 Hz. Intermediate or slow motions with frequency between 106 and 103 Hz. Very slow motions with frequency < 103 Hz. Part II: Applications: Hydrogen bonded systems: Hydrogen bond shifts. 2H quadrupolar coupling constant. Fibrous proteins: Collagen fibrils. Elastin. Cerial proteins. Silk fibroin. Keratin. Bacteriophage coat protein. Polysaccharides: Distinction of polymorphs. Network structure, dynamics and gelation mechanism. Polypeptides as new materials: Liquid crystalline polypeptides. Blend system. Globular proteins: (Almost) complete assignment of 13C NMR spectra of globular proteins. 3D structure: alpha-spectrin SH3 domain. Ligand-binding to globular protein. Membrane protein I: dynamic picture: Bacteriorhodopsin. Phoborhodopsin and its cognitive transducer. Diacylgycerol kinase. Membrane proteins II: 3D structure: 3D structure of mechanically aligned membrane proteins. Secondary structure based on distance constraints. Biologically active membrane-associated peptides: Channel-forming peptides. Antimicrobial peptides. Opioid peptides. Fusion peptides. Membrane model system. Amyloid and related biomolecules: Amyloid beta-peptide. Calcitonin (CT) |
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| Documents associés : | Autre format:
Solid state NMR spectroscopy for biopolymers |
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| 327 | 1 | |a Part I: Principles: Solid state NMR approach: CP-MAS and DD-MAS NMR |a Quadrupolar nuclei |a Brief outline of NMR parameters: Chemical shifts |a Relaxation parameters |a Dynamics-dependent suppression of peaks |a Multinuclear approaches: 31P NMR |a 2H NMR |a 17O NMR |a Experimental strategies: Isotope enrichment (labeling) |a Assignment of peaks |a Ultra high-field and ultra high-speed MAS NMR spectroscopy |a NMR constraints for structural determination: Orientational constraint |a Interatomic distance |a Torsion angles |a Conformation-dependent 13C chemical shifts |a Dynamics: Fast motions with motional frequency >106 Hz |a Intermediate or slow motions with frequency between 106 and 103 Hz |a Very slow motions with frequency < 103 Hz. Part II: Applications: Hydrogen bonded systems: Hydrogen bond shifts |a 2H quadrupolar coupling constant |a Fibrous proteins: Collagen fibrils |a Elastin |a Cerial proteins |a Silk fibroin |a Keratin |a Bacteriophage coat protein |a Polysaccharides: Distinction of polymorphs |a Network structure, dynamics and gelation mechanism |a Polypeptides as new materials: Liquid crystalline polypeptides |a Blend system |a Globular proteins: (Almost) complete assignment of 13C NMR spectra of globular proteins |a 3D structure: alpha-spectrin SH3 domain |a Ligand-binding to globular protein |a Membrane protein I: dynamic picture: Bacteriorhodopsin |a Phoborhodopsin and its cognitive transducer |a Diacylgycerol kinase |a Membrane proteins II: 3D structure: 3D structure of mechanically aligned membrane proteins |a Secondary structure based on distance constraints |a Biologically active membrane-associated peptides: Channel-forming peptides |a Antimicrobial peptides |a Opioid peptides |a Fusion peptides |a Membrane model system |a Amyloid and related biomolecules: Amyloid beta-peptide |a Calcitonin (CT) | |
| 330 | |a 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 | ||
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