Cantitate/Preț
Produs
Total produse
Vezi coșul
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 – 12 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.
Citește tot Restrânge

Din seria Methods in Enzymology

Preț: 121619 lei

Preț vechi: 166602 lei
-27% Nou

Puncte Express: 1824
Preț estimativ în valută:
23275€ • 24177$ • 19334£

Carte tipărită la comandă

Livrare economică 03-17 februarie 25

 Adaugă în coș

Wish list
Gift list
Am citit!
Adaugă în listă
Preluare comenzi: 021 569.72.76

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 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