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Biomolecular spectroscopy : advances from integrating experiments and theory /
Published continuously since 1944, Advances in Protein Chemistry and Structural Biology has been a continuous, essential resource for protein chemists. Covering reviews of methodology and research in all aspects of protein chemistry, including purification/expression, proteomics, modeling and struct...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Oxford :
Elsevier,
2013.
|
| Edición: | First edition. |
| Colección: | Advances in protein chemistry and structural biology ;
v. 93. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- Front Cover; Biomolecular Spectroscopy: Advances from Integrating Experiments and Theory; Copyright; Contents; Contributors; Introduction: Biomolecular Spectroscopy: Advances from Integrating Experiments and Theory; References; Chapter One: Studying Biomacromolecules with Two-Dimensional Infrared Spectroscopy; 1. Introduction; 1.1. Calculating 2DIR spectra from MD simulations; 2. Proteins; 2.1. Secondary structure; 2.2. Peptides and small protein domains; 2.3. Membrane proteins; 2.4. Amyloid fibrils; 3. Poly-Nucleic Acids; 4. Conclusion; Acknowledgments; Glossary; References
- Chapter Two: NMR Studies on the Dynamics of Hydrogen Bonds and Ion Pairs Involving Lysine Side Chains of Proteins1. Introduction; 2. NMR of Lysine Side-Chain Amino Groups; 2.1. 1H/15N resonances and hydrogen exchange; 2.2. Dramatic improvement of NH3+ signals by removal of scalar relaxation; 2.3. Resonance assignment of lysine NH3+ group; 3. NMR Methods to Investigate Internal Motions of Lysine NH3+ Groups; 3.1. Motional model and spectral density function; 3.2. 15N longitudinal and transverse relaxation for NH3+ groups
- 3.3. Heteronuclear nuclear Overhauser enhancement (NOE) and relaxation of 4NzHzHz terms for NH3+ groups3.4. Determination of order parameters and correlation times for internal motions; 4. NMR Methods to Investigate Hydrogen-Bonding Dynamics of Lysine NH3+ Groups; 4.1. Hydrogen-bond scalar coupling for lysine NH3+ groups; 4.2. Estimating hydrogen-bonding lifetime from bond-rotation correlation times of NH3+ groups; 5. Dynamics of Lysine Side Chains of Ubiquitin: Combined Use of NMR and Computation; 5.1. Importance of lysine side-chain NH3+ groups of ubiquitin
- 5.2. Internal motions of ubquitins lysine NH3+ groups5.3. Hydrogen-bonding dynamics of lysine NH3+ groups; 6. Ion-Pair Dynamics Involving Lysine Side Chains and Their Role in Protein-DNA Association; 6.1. Contact ion-pair (CIP) and solvent-separated ion-pair (SIP) states; 6.2. Mobility of Lys NH3+ groups in ion pairs with DNA; 6.3. Hydrogen-bonding dynamics of the interfacial ion pairs; 6.4. How can dithioation of DNA phosphate enhance protein-DNA association?; 7. Conclusions and Future Perspectives; Acknowledgment; References
- Chapter Three: Structure-Function Relationship of the Plant Photosynthetic Pigment-Protein Complex LHCII Studied with Mol ... 1. Photosynthetic Antenna Function; 2. Spectroscopic Studies on Photoprotection in LHCII; 3. Conclusions; Acknowledgments; References; Chapter Four: Combined Use of Optical Spectroscopy and Computational Methods to Study the Binding and the Photoinduced Co ... ; 1. Introduction; 2. Photoactive Ligands; 3. Protein Involvement; 4. Nature-Mimicking Approach; 5. Challenge of Artificial Approaches: Reversibility