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Solid State NMR Spectroscopy for Biopolymers Hazime Sait

Solid State NMR Spectroscopy for Biopolymers By Hazime Sait

Solid State NMR Spectroscopy for Biopolymers by Hazime Sait


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Summary

‘‘Biopolymers’’ are polymeric materials of biological origin, including globular, membrane, and fibrous proteins, polypeptides, nucleic acids, po- saccharides, lipids, etc.

Solid State NMR Spectroscopy for Biopolymers Summary

Solid State NMR Spectroscopy for Biopolymers: Principles and Applications by Hazime Sait

‘‘Biopolymers’’ are polymeric materials of biological origin, including globular, membrane, and fibrous proteins, polypeptides, nucleic acids, po- saccharides, lipids, etc. and their assembly, although preference to respe- ive subjects may be different among readers who are more interested in their biological significance or industrial and/or medical applications. Nevert- less, characterizing or revealing their secondary structure and dynamics may be an equally very important and useful issue for both kinds of readers. Special interest in revealing the 3D structure of globular proteins, nucleic acids, and peptides was aroused in relation to the currently active Structural Biology. X-ray crystallography and multidimensional solution NMR sp- troscopy have proved to be the standard and indispensable means for this purpose. There remain, however, several limitations to this end, if one intends to expand its scope further. This is because these approaches are not always straightforward to characterize fibrous or membrane proteins owing to extreme difficulty in crystallization in the former, and insufficient spectral resolution due to sparing solubility or increased effective molecular mass in the presence of surrounding lipid bilayers in the latter.

Solid State NMR Spectroscopy for Biopolymers Reviews

From the reviews:

"This book surveys much of the current research in the area of biological solid-state NMR spectroscopy, and as such should be of great interest to the chemical, biochemical, and biophysical communities. The level is appropriate for graduate students, and the book would be an excellent textbook for a graduate level course in biological solid-state NMR spectroscopy. Its publication is timely considering the recent numerous developments in this area … ." (Michele Auger, Journal of the American Chemical Society, Vol. 129 (10), 2007)

Table of Contents

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)

Additional information

NPB9781402043024
9780710626912
0710626916
Solid State NMR Spectroscopy for Biopolymers: Principles and Applications by Hazime Sait
New
Hardback
Springer-Verlag New York Inc.
2006-07-05
455
N/A
Book picture is for illustrative purposes only, actual binding, cover or edition may vary.
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