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Protein NMR for the Millennium is the third volume in a special thematic series devoted to the latest developments in protein NMR under the Biological Magnetic Resonance umbrella. This book is divided into three major sections dealing with significant recent advances in the study of large proteins in solution and solid state, structure refinement, and screening of bioactive ligands.
Key Features:
- TROSY,
- Segmental isotope labeling of proteins,
- Hydrogen bond scalar couplings,
- Structure refinement based on residual dipolar couplings,
- Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.
Table des matières
Transverse Relaxation Optimized Spectroscopy.- Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins.- Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach.- Global Fold Determination of Large Proteins using Site-Directed Spin Labeling.- Solid State NMR Studies of Uniformly Isotopically Enriched Proteins.- NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids.- Angular Restraints from Residual Dipolar Couplings for Structure Refinement.- Protein Structure Refinement using Residual Dipolar Couplings.- Hydrogen Bond Scalar Couplings - A New Tool In Biomolecular NMR.- NMR Methods for Screening the Binding of Ligands to Proteins - Identification and Characterization of Bioactive Ligands.
A propos de l'auteur
Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR).
Résumé
Protein NMR for the Millennium is the third volume in a special thematic series devoted to the latest developments in protein NMR under the Biological Magnetic Resonance umbrella. This book is divided into three major sections dealing with significant recent advances in the study of large proteins in solution and solid state, structure refinement, and screening of bioactive ligands.
Key Features:
- TROSY,
- Segmental isotope labeling of proteins,
- Hydrogen bond scalar couplings,
- Structure refinement based on residual dipolar couplings,
- Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.
Texte suppl.
`The book is generally easy to read for those with an appreciable knowledge of protein NMR spectroscopy. [...]presents a timely review of many recently developed techniques for the study of large proteins by NMR spectroscopy. We highly recommend it as a reference for anyone with an active interest in this field.'
Journal of the American Chemical Society, 125:51 (2003)
Commentaire
`The book is generally easy to read for those with an appreciable knowledge of protein NMR spectroscopy. [...]presents a timely review of many recently developed techniques for the study of large proteins by NMR spectroscopy. We highly recommend it as a reference for anyone with an active interest in this field.'
Journal of the American Chemical Society, 125:51 (2003)
