Overview

Full Product Details

Author:   Thomas L. James (School of Pharmacy, 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.) ,  Uli Schmitz
Publisher:   Elsevier Science Publishing Co Inc
Imprint:   Academic Press Inc
Volume:   v. 339
Dimensions:   Width: 15.20cm , Height: 2.70cm , Length: 22.90cm
Weight:   0.770kg
ISBN:  

9780121822408

ISBN 10:   0121822400
Pages:   454
Publication Date:   12 July 2001
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Hardback
Publisher's Status:   Out of Print
Availability:   In Print  
Limited stock is available. It will be ordered for you and shipped pending supplier's limited stock.

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 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

Reviews

Author Information

Tab Content 6

Author Website:  

Customer Reviews

Recent Reviews

No review item found!

Add your own review!

Countries Available

All regions