Nantilus
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...
Enregistré dans:
| 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 : |
Accès Nantes Université
Accès direct soit depuis les campus via le réseau ou le wifi eduroam soit à distance avec un compte @etu.univ-nantes.fr ou @univ-nantes.fr |
| Note sur l'URL : | Accès sur la plateforme de l'éditeur Accès sur la plateforme Istex |
| Condition d'utilisation et de reproduction : | Conditions particulières de réutilisation pour les bénéficiaires des licences nationales : https://www.licencesnationales.fr/springer-nature-ebooks-contrat-licence-ln-2017 |
| 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) |
| Sujets : | |
| Documents associés : | Autre format:
Solid state NMR spectroscopy for biopolymers |