Nuclear Magnetic Resonance of Biological Macromolecules, Part B

Thomas L. James, Volker Dotsch, Uli Schmitz (Herausgeber)

Buch | Hardcover

454 Seiten

2001
Academic Press Inc (Verlag)
978-0-12-182240-8 (ISBN)

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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 experi

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

Erscheint lt. Verlag	12.7.2001
Reihe/Serie	Methods in Enzymology
Verlagsort	San Diego
Sprache	englisch
Maße	152 x 229 mm
Gewicht	770 g
Themenwelt	Naturwissenschaften ► Biologie ► Biochemie
ISBN-10	0-12-182240-0 / 0121822400
ISBN-13	978-0-12-182240-8 / 9780121822408
Zustand	Neuware