Solid State NMR Spectroscopy for Biopolymers (eBook)

Principles and Applications
eBook Download: PDF
2006 | 2006
XIII, 455 Seiten
Springer Netherland (Verlag)
978-1-4020-4303-1 (ISBN)

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Solid State NMR Spectroscopy for Biopolymers - Hazime Saitô, Isao Ando, Akira Naito
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''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.
''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.

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  
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)

Erscheint lt. Verlag 5.8.2006
Zusatzinfo XIII, 455 p.
Verlagsort Dordrecht
Sprache englisch
Themenwelt Naturwissenschaften Biologie
Naturwissenschaften Chemie Analytische Chemie
Naturwissenschaften Chemie Physikalische Chemie
Naturwissenschaften Physik / Astronomie
Technik Maschinenbau
Wirtschaft
Schlagworte 3D structure • Biopolymer • Crystal • Dynamics • liquid • Membrane-associated peptides • Membrane Proteins • Nuclear Magnetic Resonance (NMR) • Polymer • Solid State NMR • spectroscopy
ISBN-10 1-4020-4303-1 / 1402043031
ISBN-13 978-1-4020-4303-1 / 9781402043031
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