Saitô / Naito / Ando | Solid State NMR Spectroscopy for Biopolymers | Buch | 978-1-4020-4302-4 | sack.de

Buch, Englisch, 455 Seiten, HC runder Rücken kaschiert, Format (B × H): 160 mm x 241 mm, Gewicht: 863 g

Saitô / Naito / Ando

Solid State NMR Spectroscopy for Biopolymers

Principles and Applications

Buch, Englisch, 455 Seiten, HC runder Rücken kaschiert, Format (B × H): 160 mm x 241 mm, Gewicht: 863 g

ISBN: 978-1-4020-4302-4
Verlag: Springer Netherlands


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. Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. Special efforts have been made to include 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 simplest DD-MAS 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 and intermediate fluctuation motions can be revealed easily by specific suppression of peaks.

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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:P NMR.- H NMR.- O 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 C chemical shifts.- Dynamics: Fast motions with motional frequency >10 Hz.- Intermediate or slow motions with frequency between 10 and 10 Hz.- Very slow motions with frequency < 10 Hz.

Part II: Applications:

Hydrogen bonded systems: Hydrogen bond shifts.- H 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 C 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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