Protein NMR Spectroscopy
Practical Techniques and Applications
Herausgegeben von Roberts, Gordon; Lian, Lu-Yun
Protein NMR Spectroscopy
Practical Techniques and Applications
Herausgegeben von Roberts, Gordon; Lian, Lu-Yun
- Gebundenes Buch
- Merkliste
- Auf die Merkliste
- Bewerten Bewerten
- Teilen
- Produkt teilen
- Produkterinnerung
- Produkterinnerung
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique in structural biology for obtaining high resolution 3-D structures of proteins, second only, and complementary to X-ray crystallography. Molecules are studied in solution, where conditions are closer to what is found in the cell. It is the primary technique used to obtain information on intrinsically disordered (unfolded) proteins, since these proteins will not crystallize easily.
The aim of this book is to provide the newcomer to NMR techniques with practical guidance on how to choose the right experiment, how to carry…mehr
- Oliver ZerbeApplied NMR Spectroscopy for Chemists and Life Scientists49,99 €
- Stefan BergerNMR Spectroscopy of the Non-Metallic Elements1.175,99 €
- Protein Surface Recognition176,99 €
- Roderick E WasylishenNMR of Quadrupolar Nuclei in Solid Materials201,99 €
- Daniel CanetNuclear Magnetic Resonance212,99 €
- David M. Grant / Robin K. Harris (Hgg.)Encyclopedia of Nuclear Magnetic Resonance, Volume 11.535,99 €
- Medical Imaging Based on Magnetic Fields and Ultrasounds184,99 €
-
-
-
The aim of this book is to provide the newcomer to NMR techniques with practical guidance on how to choose the right experiment, how to carry out the experiment, and how to analyse the resulting spectra. Those who are familiar with the chemical applications of NMR will also find it helpful in describing the special requirements of proteins.
- Produktdetails
- Verlag: Wiley & Sons
- Artikelnr. des Verlages: 14572193000
- 1. Auflage
- Seitenzahl: 368
- Erscheinungstermin: 8. August 2011
- Englisch
- Abmessung: 253mm x 179mm x 24mm
- Gewicht: 810g
- ISBN-13: 9780470721933
- ISBN-10: 0470721936
- Artikelnr.: 33090177
- Verlag: Wiley & Sons
- Artikelnr. des Verlages: 14572193000
- 1. Auflage
- Seitenzahl: 368
- Erscheinungstermin: 8. August 2011
- Englisch
- Abmessung: 253mm x 179mm x 24mm
- Gewicht: 810g
- ISBN-13: 9780470721933
- ISBN-10: 0470721936
- Artikelnr.: 33090177
References 4 1 Sample Preparation, Data Collection and Processing 5
Frederick W. Muskett 1.1 Introduction 5 1.2 Sample Preparation 5 1.3 Data
Collection 11 1.4 Data Processing 17 2 Isotope Labelling 23 Mitsuhiro
Takeda and Masatsune Kainosho 2.1 Introduction 23 2.2 Production Methods
for Isotopically Labelled Proteins 24 2.3 Uniform Isotope Labelling of
Proteins 29 2.4 Selective Isotope Labelling of Proteins 32 2.5 Segmental
Labelling 37 2.6 SAIL Methods 38 2.7 Concluding Remarks 45 3 Resonance
Assignments 55 Lu-Yun Lian and Igor L. Barsukov 3.1 Introduction 55 3.2
Resonance Assignment of Unlabelled Proteins 56 3.3 15N-Edited Experiments
60 3.4 Triple Resonance 62 3.5 Side-Chain Assignments 77 4 Measurement of
Structural Restraints 83 Geerten W. Vuister, Nico Tjandra, Yang Shen, Alex
Grishaev and Stephan Grzesiek 4.1 Introduction 83 4.2 NOE-Based Distance
Restraints 84 4.3 Dihedral Restraints Derived from J-Couplings 96 4.4
Hydrogen Bond Restraints 103 4.5 Orientational Restraints 107 4.6 Chemical
Shift Structural Restraints 129 4.7 Solution Scattering Restraints 137 5
Calculation of Structures from NMR Restraints 159 Peter Guntert 5.1
Introduction 159 5.2 Historical Development 161 5.3 Structure Calculation
Algorithms 164 5.4 Automated NOE Assignment 173 5.5 Nonclassical Approaches
178 5.6 Fully Automated Structure Analysis 181 6 Paramagnetic Tools in
Protein NMR 193 Peter H.J. Keizers and Marcellus Ubbink 6.1 Introduction
193 6.2 Types of Restraints 194 6.3 What Metals to Use? 200 6.4
Paramagnetic Probes 203 6.5 Examples 209 6.6 Conclusions and Perspective
212 7 Structural and Dynamic Information on Ligand Binding 221 Gordon
Roberts 7.1 Introduction 221 7.2 Fundamentals of Exchange Effects on NMR
Spectra 222 7.3 Measurement of Equilibrium and Rate Constants 229 7.4
Detecting Binding - NMR Screening 238 7.5 Mechanistic Information 241 7.6
Structural Information 246 8 Macromolecular Complexes 269 Paul C. Driscoll
8.1 Introduction 269 8.2 Spectral Simplification through Differential
Isotope Labelling 270 8.3 Basic NMR Characterisation of Complexes 273 8.4
3D Structure Determination of Macromolecular Protein-Ligand Complexes 277
8.5 Literature Examples 297 9 Studying Partially Folded and Intrinsically
Disordered Proteins Using NMR Residual Dipolar Couplings 319 Malene
Ringkjøbing Jensen, Valery Ozenne, Loic Salmon, Gabrielle Nodet, Phineus
Markwick, Pau Bernadö and Martin Blackledge 9.1 Introduction 319 9.2
Ensemble Descriptions of Unfolded Proteins 320 9.3 Experimental Techniques
for the Characterisation of IDPs 320 9.4 NMR Spectroscopy of Intrinsically
Disordered Proteins 321 9.5 Residual Dipolar Couplings 323 9.6 Conclusions
340 References 340 Index 347
References 4 1 Sample Preparation, Data Collection and Processing 5
Frederick W. Muskett 1.1 Introduction 5 1.2 Sample Preparation 5 1.3 Data
Collection 11 1.4 Data Processing 17 2 Isotope Labelling 23 Mitsuhiro
Takeda and Masatsune Kainosho 2.1 Introduction 23 2.2 Production Methods
for Isotopically Labelled Proteins 24 2.3 Uniform Isotope Labelling of
Proteins 29 2.4 Selective Isotope Labelling of Proteins 32 2.5 Segmental
Labelling 37 2.6 SAIL Methods 38 2.7 Concluding Remarks 45 3 Resonance
Assignments 55 Lu-Yun Lian and Igor L. Barsukov 3.1 Introduction 55 3.2
Resonance Assignment of Unlabelled Proteins 56 3.3 15N-Edited Experiments
60 3.4 Triple Resonance 62 3.5 Side-Chain Assignments 77 4 Measurement of
Structural Restraints 83 Geerten W. Vuister, Nico Tjandra, Yang Shen, Alex
Grishaev and Stephan Grzesiek 4.1 Introduction 83 4.2 NOE-Based Distance
Restraints 84 4.3 Dihedral Restraints Derived from J-Couplings 96 4.4
Hydrogen Bond Restraints 103 4.5 Orientational Restraints 107 4.6 Chemical
Shift Structural Restraints 129 4.7 Solution Scattering Restraints 137 5
Calculation of Structures from NMR Restraints 159 Peter Guntert 5.1
Introduction 159 5.2 Historical Development 161 5.3 Structure Calculation
Algorithms 164 5.4 Automated NOE Assignment 173 5.5 Nonclassical Approaches
178 5.6 Fully Automated Structure Analysis 181 6 Paramagnetic Tools in
Protein NMR 193 Peter H.J. Keizers and Marcellus Ubbink 6.1 Introduction
193 6.2 Types of Restraints 194 6.3 What Metals to Use? 200 6.4
Paramagnetic Probes 203 6.5 Examples 209 6.6 Conclusions and Perspective
212 7 Structural and Dynamic Information on Ligand Binding 221 Gordon
Roberts 7.1 Introduction 221 7.2 Fundamentals of Exchange Effects on NMR
Spectra 222 7.3 Measurement of Equilibrium and Rate Constants 229 7.4
Detecting Binding - NMR Screening 238 7.5 Mechanistic Information 241 7.6
Structural Information 246 8 Macromolecular Complexes 269 Paul C. Driscoll
8.1 Introduction 269 8.2 Spectral Simplification through Differential
Isotope Labelling 270 8.3 Basic NMR Characterisation of Complexes 273 8.4
3D Structure Determination of Macromolecular Protein-Ligand Complexes 277
8.5 Literature Examples 297 9 Studying Partially Folded and Intrinsically
Disordered Proteins Using NMR Residual Dipolar Couplings 319 Malene
Ringkjøbing Jensen, Valery Ozenne, Loic Salmon, Gabrielle Nodet, Phineus
Markwick, Pau Bernadö and Martin Blackledge 9.1 Introduction 319 9.2
Ensemble Descriptions of Unfolded Proteins 320 9.3 Experimental Techniques
for the Characterisation of IDPs 320 9.4 NMR Spectroscopy of Intrinsically
Disordered Proteins 321 9.5 Residual Dipolar Couplings 323 9.6 Conclusions
340 References 340 Index 347