Saitô / Ando / Naito Solid State NMR Spectroscopy for Biopolymers

Principles and Applications
1. Auflage 2006
ISBN: 978-1-4020-4303-1
Verlag: Springer Netherland
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 455 Seiten, eBook

‘‘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.

Zielgruppe

Research

Autoren/Hrsg.

Saitô, Hazime

Ando, Isao

Naito, Akira

Inhaltsverzeichnis

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:31
P NMR.-
2
H NMR.-
17
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
13
C chemical shifts.-
Dynamics:
Fast motions with motional frequency >10
6
Hz.- Intermediate or slow motions with frequency between 10
6
and 10
3
Hz.- Very slow motions with frequency < 10
3
Hz.
Part II: Applications: Hydrogen bonded systems:
Hydrogen bond shifts.-
2
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
13
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).