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...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Livre numérique |
| Kieli: | Anglais |
| Julkaistu: |
Dordrecht :
Springer Netherlands
[20..].
Cham : Springer Nature |
| Painos: | 1st ed. 2006. |
| Linkit: | Accès sur la plateforme de l'éditeur Accès sur la plateforme Istex Accès Université d'Orléans Accès INSA CVL |
| Huomautus: |
Archives Springer e-books (Licence nationale) Archives Springer e-books (Licence nationale) |
| Autres localisations: | Voir dans le Sudoc |
| Edition sous un autre format: | • Solid state NMR spectroscopy for biopolymers, principles and applications, Hazime Saitô,... Isao Ando,... Akira Naito,..., Dordrecht, Springer, 2006, 1 vol. (XIII-464 p.), 978-1-4020-4302-4 |
Sisällysluettelo:
- 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)