Hazime Saitô, Isao Ando, Akira Naito

Solid State NMR Spectroscopy for Biopolymers (eBook, PDF)

Principles and Applications

• Format: PDF

Produktbeschreibung

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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Produktdetails

• Verlag: Springer Netherlands
• Seitenzahl: 455
• Erscheinungstermin: 5. August 2006
• Englisch
• ISBN-13: 9781402043031
• Artikelnr.: 37339453

Autorenporträt

Hazime Saitô, Hiroshima University, Higashi-Hiroshima, Japan / Isao Ando, Tokyo Institute of Technology, Japan / Akira Naito, Yokohama National University, Japan

Inhaltsangabe

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: ³¹P NMR.- ²H NMR.- ¹⁷O 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 ¹³C chemical shifts.- Dynamics: Fast motions with motional frequency >10⁶ Hz.- Intermediate or slow motions with frequency between 10⁶ and 10³ Hz.- Very slow motions with frequency < 10³ Hz.



Part II: Applications:

Hydrogen bonded systems: Hydrogen bond shifts.- ²H 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 ¹³C 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).

Rezensionen

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)