Solid State NMR Spectroscopy for Biopolymers: Principles and Applications

ISBN-13: 9781402043024 / Angielski / Twarda / 2006 / 455 str.

Hazime Saito; Isao Ando; Akira Naito

Opis

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."

Recenzje

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)

Spis treści

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)

Blurb

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 industrial and medical applications of biopolymers, it is crucial to know details of their secondary structure, dynamics and assembly. The biopolymers include globular, membrane and fibrous proteins, polypeptides, nucleic acids, polysaccharides and lipids. Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. The major advantage of solid state NMR spectroscopy is that the resulting line widths can be manipulated experimentally and are not influenced by motional fluctuation of proteins under consideration as a whole.

Solid State NMR Spectroscopy for Biopolymers: Principles and Applications provides a comprehensive account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR spectroscopy. Special efforts have been made towards 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 most simple DD-MAS (one pulse excitation with high power decoupling) 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 (10⁸ Hz) and intermediate (10⁴ -10⁵ Hz) fluctuation motions can be revealed easily by specific suppression of peaks.

This book is an invaluable resource for biophysicists, biochemists and chemists, including NMR spectroscopists, structural biologists, and polymer scientists. The book provides an introduction suitable for graduate students as well as for research scientists, including those working in the pharmaceutical and chemical industries.