Hazime Saitô, Isao Ando, Akira Naito

Solid State NMR Spectroscopy for Biopolymers (eBook, PDF)

Principles and Applications

• Format: PDF

Produktbeschreibung

‘‘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.

Produktdetails

• Verlag: Springer Netherland
• 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).

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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)