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)

• 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).

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)

• 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).

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)

• 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).