Nuclear Magnetic Resonance of Biological Macromolecules, Part B by Thomas L. JamesNuclear Magnetic Resonance of Biological Macromolecules, Part B by Thomas L. James

Nuclear Magnetic Resonance of Biological Macromolecules, Part B

byThomas L. JamesEditorVolker Dotsch, Uli Schmitz

Hardcover | March 23, 1992

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This volume and its companion,Volume 338 , supplementVolumes 176, 177, 239 , and261 . 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.
Title:Nuclear Magnetic Resonance of Biological Macromolecules, Part BFormat:HardcoverDimensions:454 pages, 9 × 6 × 0.98 inPublished:March 23, 1992Publisher:Academic PressLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:0121822400

ISBN - 13:9780121822408

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Table of Contents

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-Specific15N 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