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

Nuclear Magnetic Resonance of Biological Macromolecules, Part B: Methods in Enzymology, cartea 339

Thomas L. James, Volker Dotsch, Uli Schmitz
en Limba Engleză Hardback – 11 iul 2001
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.
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Specificații

ISBN-13: 9780121822408
ISBN-10: 0121822400
Pagini: 454
Dimensiuni: 152 x 229 x 27 mm
Greutate: 0.83 kg
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology

Public țintă

Biochemists, biophysicists, molecular biologists, and cell biologists.

Cuprins

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