Saitô / Naito / Ando | Solid State NMR Spectroscopy for Biopolymers | Buch | 978-90-481-7100-2 | www.sack.de

Buch, Englisch, 455 Seiten, Previously published in hardcover, Format (B × H): 160 mm x 240 mm, Gewicht: 760 g

Saitô / Naito / Ando

Solid State NMR Spectroscopy for Biopolymers

Principles and Applications
1. Auflage. Softcover version of original hardcover Auflage 2006
ISBN: 978-90-481-7100-2
Verlag: Springer Netherlands

Principles and Applications

Buch, Englisch, 455 Seiten, Previously published in hardcover, Format (B × H): 160 mm x 240 mm, Gewicht: 760 g

ISBN: 978-90-481-7100-2
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

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 shifts
 3.2. Relaxation parameters
 3.3. Dynamics-dependent suppression of peaks

4. Multinuclear approaches
 4.1. 31P NMR
 4.2. 2H NMR 
 4.3. 17O 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 spectroscopy

6. NMR constraints for structural determination 
 6.1. Orientational constraint
 6.2. Interatomic distance
 6.3. Torsion angles
 6.4. Conformation-dependent 13C chemical shifts 

7. Dynamics
 7.1. Fast motions with motional frequency >106 Hz
 7.2. Intermediate or slow motions with frequency between 106 and 103 Hz
 7.3. Very slow motions with frequency < 103 Hz
 

Part II  Applications

8. Hydrogen bonded systems
 8.1. Hydrogen bond shifts
 8.2. 2H quadrupolar coupling constant         

9. Fibrous proteins            
 9.1. Collagen fibrils 
 9.2. Elastin
 9.3. Cerial proteins
 9.4. Silk fibroin
 9.5. Keratin
 9.6.      Bacteriophage coat protein

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 13C NMR spectra of globular proteins
 12.2. 3D structure: ?-spectrin SH3 domain
 12.3. Ligand-binding to globular protein

13. Membrane protein I: dynamic picture  
 13.1. Bacteriorhodopsin
 13.2. Phoborhodopsin and its cognitive transducer
 13.3. Diacylgycerol kinase

14. Membrane proteins II: 3D structure 
 14.1. 3D structure of mechanically aligned membrane proteins
 14.2. Secondary structure based on distance constraints

15. Biologically active membrane-associated peptides
 15.1. Channel-forrming peptides
 15.2. Antimicrobial peptides
 15.3. Opioid peptides
 15.4. Fusion peptides
 15.5. Membrane model system                        

17. Amyloid and related biomolecules
 17.1. Amyloid ?-peptide
 17.2. Calcitonin (CT)



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