Nuclear Magnetic Resonance of Biological Macromolecules, Part B

by Thomas L. James (Editor), Volker Dotsch (Editor), Uli Schmitz (Editor)

Overview

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.

Product Details

ISBN-13:	9780080496894
Publisher:	Elsevier Science & Technology Books
Publication date:	07/12/2001
Series:	Methods in Enzymology , #339
Sold by:	Barnes & Noble
Format:	eBook
Pages:	454
File size:	17 MB
Note:	This product may take a few minutes to download.

About the Author

AUTHORBIOS: Thomas L. James, University of California, San Francisco, U.S.A.
Volker Dotsch, University of California, San Francisco, U.S.A.
Uli Schmitz, Gemlabs Technologies, Inc., Redwood City, California, U.S.A.

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-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 β-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

Editorial Reviews

The Methods in Enzymology series represents the gold-standard.

Neuroscience

Incomparably useful.

Analytical Biochemistry

It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page.

Bio/Technology