Nuclear magnetic resonance of biological macromolecules. Volume 394, Part C /

• Άλλοι συγγραφείς: James, Thomas L.
• Μορφή: Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: San Diego, CA : Academic Press, ©2005.
• Σειρά: Methods in enzymology ; volume 394.
• Θέματα: Nuclear magnetic resonance.; Macromolecules.; SCIENCE > Life Sciences > Biochemistry.; Magnetic Resonance Spectroscopy > methods.; Macromolecular Substances.; Polymers > chemistry.; Proteins > chemistry.; Electronic books.

 The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules. * One of the most highly respected publications in the field of biochemistry since 1955 * Frequently consulted, and praised by researchers and reviewers alike * Truly an essential publication for anyone in any field of the life sciences. 

 Identification and optimization of protein domains for NMR studies -- In-cell NMR spectroscopy -- Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining -- Cross-correlated relaxation for structure and dynamics -- Rapid NMR Data Collection -- An Integrated Platform for Automated Analysis of Protein NMR Structures -- Rapid Assessment of Protein Structural Stability and Fold Validation via NMR -- Determination of Protein Backbone Structures from Residual Dipolar Couplings -- Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium -- Protein Structure Estimation From Minimal Restraints Using Rosetta -- Protein Structure Elucidation From Minimal Data: The CLOUDS and ABACUS Approaches -- Elucidation of the Protein Folding Landscape by NMR -- Membrane Protein Preparation for TROSY NMR Screening -- Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP -- NMR Experiments on Aligned Samplet of Membrane Proteins -- NMR techniques used with very large biological macromolecules in solution -- Structure determination of large biological RNAs -- Hydrodynamic Models and Computational Methods for NMR relaxation -- Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High Molecular Weight Systems -- Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for RNA -- NMR techniques for identifying the interface of a larger protein-protein complex: cross and transferred cross-saturation experiments -- Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy -- Structure determination of protein/RNA complexes by NMR -- Utilization of NMR-derived fragment leads in drug design -- Discovery of Ligands by a Combination of Computational and NMR-based Screening: RNA as an Example Target.