Nuclear Magnetic Resonance of Biological Macromolecules, Part B

This volume and its companion, Volume 338, supplement Volumes 176, 177, 239, and 261. Chapters are 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.

Section I: Proteins A. Techniques for proteins

[1]: Physiological Conditions and Practicality for Protein Nuclear Magnetic Resonance Spectroscopy: Experimental Methodologies and Theoretical Background

[2]: Optimization of Protein Solubility and Stability for Protein Nuclear Magnetic Resonance

[3]: Segmental Isotopic Labeling Using Expressed Protein Ligation

[4]: High-Resolution Nuclear Magnetic Resonance of Encapsulated Proteins Dissolved in Low Viscosity Fluids

[5]: Automated Assignment of Ambiguous Nuclear Overhauser Effects with ARIA

[6]: Automatic Determination of Protein Backbone Resonance Assignments from Triple Resonance Nuclear Magnetic Resonance Data

[7]: Nuclear Magnetic Resonance Relaxation in Determination of Residue-Specific ¹⁵N Chemical Shift Tensors in Proteins in Solution: Protein Dynamics, Structure, and Applications of Transverse Relaxation Optimized Spectroscopy

[8]: Dipolar Couplings in Macromolecular Structure Determination

[9]: Nuclear Magnetic Resonance Methods for High Molecular Weight Proteins: A Study Involving a Complex of Maltose Binding Protein and ß-Cyclodextrin

[10]: Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules

Section I: Proteins B. Classes of proteins

[11]: Characterizing Protein-Protein Complexes and Oligomers by Nuclear Magnetic Resonance Spectroscopy

[12]: Nuclear Magnetic Resonance Methods for Elucidation of Structure and Dynamics in Disordered States

[13]: Micellar Systems as Solvents in Peptide and Protein Structure Determination

[14]: Nuclear Magnetic Resonance of Membrane-Associated Peptides and Proteins

[15]: Paramagnetic Probes in Metalloproteins

Section II: Macromolecular complexes

[16]: Protein–DNA Interactions

[17]: Nuclear Magnetic Resonance Methods to Study Structure and Dynamics of RNA–Protein Complexes

[18]: Protein–protein interactions probed by nuclear magnetic resonance spectroscopy

[19]: Solid-State Nuclear Magnetic Resonance Techniques for Structural Studies of Amyloid Fibrils

Author Index

Subject Index