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Annual Reports on NMR Spectroscopy. Vol. 83 /
Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules. In recent years, no other technique has gained such significance as NMR spectroscopy. It is used in all branches of science in which precise structural determinati...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Burlington :
Elsevier Science,
2014.
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| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- 4. Micro- to Millisecond Motions: Solid State NMR4.1. Dynamic Interference: SRI; 4.2. CODEX and Chemical Exchange; 4.3. Order Parameters Based on DCs; 4.4. Relaxation Rate parameters: R1, R2, and R1; 4.5. Lineshape Analysis; 5. Very Slow Motions: 1D MAS Exchange; 6. Globular Proteins; 6.1. Comparison of Protein Dynamics Between Solution and Solid; 6.2. Pico- to Nanosecond motions: Conformational Entropy and Allostery; 6.3. ms-s Motions: Biological Function; 6.3.1. Protein Folding; 6.3.2. Catalysis and Allosteric Regulation; 7. Membrane Proteins; 7.1. Retinal Proteins
- 7.1.1. Bacteriorhodopsin ([beta]R)7.1.2. Sensory Rhodopsin and Proteorhodopsin; 7.2. Other Proteins; 8. Conclusion; Acknowledgements; References; Chapter Two: Recent Progress in the Solid-State NMR Studies of Short Peptides: Techniques, Structure and Dynamics; 1. Introduction; 2. Development of the New Solid-State NMR Techniques Useful in Structural Studies of Peptides; 2.1. 1H Solid-State NMR; 2.2. 13C and 15N Sensitivity under Fast and Medium Magic-Angle Spinning; 2.3. Two-Dimensional Correlations under F-MAS; 2.3.1. 1H-13C and 1H-15N HETCOR Correlations
- 2.3.2. 13C-13C and 15N-15N HOMCOR Correlations2.4. Quadrupolar Nuclei; 3. Molecular Dynamics of Peptides in the Solid State; 3.1. Probing the Dynamics in Different Time Scales; 3.2. Tools for Analysis of the Local Molecular Motions of Peptides in the Solid State; 3.2.1. Relaxation Times; 3.2.2. Chemical Shift Anisotropy; 3.2.3. Investigation of the Dynamics by Deuterium Solid-State NMR: Line-Shape Analysis; 3.2.4. Heteronuclear Dipolar Recoupling Sequences; 4. Polymorphism and Solvatomorphism of Peptides; 4.1. Solid-State NMR Study of Polymorphs and Solvatomorphs
- 4.1.1. Ala-Ala-Ala Tripeptide-The Case Study5. Complementarity of Theoretical and NMR Methods in Assignment of the Solid-State Structure of Peptides; 5.1. Techniques Used for Calculations of NMR Parameters in the Solid State; 5.2. Theoretical Methods as a Tool for Structure Assignment of Peptides in the Solid State; 5.3. Fine Refinement of Peptide Crystals with Molecular Disorder; 5.4. Theoretical Methods Versus Molecular Motion; 6. Concluding Remarks; Acknowledgement; References; Chapter Three: Solid-State 17O NMR Studies of Biomolecules; 1. Introduction; 2. NMR Tensor Parameters