Format:
Online-Ressource (XXXII, 454 S.)
ISBN:
0121822400
,
9780121822408
Series Statement:
Methods in enzymology 339
Content:
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.
Content:
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
Note:
Description based upon print version of record
,
Front Cover; Nuclear Magnetic Resonance of Biological Macromolecules; Copyright Page; Tabel of Contents; Contributors to Volume 339; Preface; Volume in Series; Section I: Proteins; A. Techniques for Proteins; Chapter 1. Physiological Conditions and Practicality for Protein Nuclear Magnetic Resonance Spectroscopy: Experimental Methodologies and Theoretical Background; Chapter 2. Optimization of Protein Solubility and Stability for Protein Nuclear Magnetic Resonance; Chapter 3. Segmental Isotopic Labeling Using Expressed Protein Ligation
,
Chapter 4. High-Resolution Nuclear Magnetic Resonance of Encapsulated Proteins Dissolved in Low Viscosity FluidsChapter 5. Automated Assignment of Ambiguous Nuclear Overhauser Effects with ARIA; Chapter 6. Automatic Determination of Protein Backbone Resonance Assignments from Triple Resonance Nuclear Magnetic Resonance Data; Chapter 7. Nuclear Magnetic Resonance Relaxation in Determination of Residue-Specific 15N Chemical Shift Tensors in Proteins in Solution: Protein Dynamics, Structure, and Applications ofTransverse Relaxation Optimized Spectroscopy
,
Chapter 8. Dipolar Couplings in Macromolecular Structure DeterminationChapter 9. Nuclear Magnetic Resonance Methods for High Molecular Weight Proteins: A Study Involving a Complex of Maltose Binding Protein and ß-Cyclodextrin; Chapter 10. Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules; B. Classes of Proteins; Chapter 11. Characterizing Protein-Protein Complexes and Oligomers by Nuclear Magnetic Resonance Spectroscopy; Chapter 12. Nuclear Magnetic Resonance Methods for Elucidation of Structure and Dynamics in Disordered States
,
Chapter 13. Micellar Systems as Solvents in Peptide and Protein Structure DeterminationChapter 14. Nuclear Magnetic Resonance of Membrane- Associated Peptides and Proteins; Chapter 15. Paramagnetic Probes in Metalloproteins; Section II: Macromolecular Complexes; Chapter 16. Protein-DNA Interactions; Chapter 17. Nuclear Magnetic Resonance Methods to Study Structure and Dynamics of RNA-Protein Complexes; Chapter 18. Protein-Protein Interactions Probed by Nuclear Magnetic Resonance Spectroscopy
,
Chapter 19. Solid-State Nuclear Magnetic Resonance Techniques for Structural Studies of Amyloid FibrilsAuthor Index; Subject Index;
,
Literaturangaben
In:
Pt. B
Additional Edition:
Erscheint auch als Druck-Ausgabe Nuclear magnetic resonance of biological macromolecules ; Pt. B San Diego, Calif. [u.a.] : Acad. Press, 2001 ISBN 0121822400
Language:
English
Keywords:
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