Protein NMR spectroscopy principles and practice

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Veröffentlicht: Amsterdam [u.a.] Academic Press 2007
Ausgabe:2. ed.
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Datensatz im Suchindex

DE-BY-TUM_call_number 1002/CHE 820f 2010 A 6200(2)
0302/CHE 820f 1996 A 2153(2)
DE-BY-TUM_katkey 1725650
DE-BY-TUM_media_number 040008284357
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adam_text Contents Preface V Preface to the First Edition vii Acknowledgements xi CHAPTER Classical NMR Spectroscopy 1.1 2 1.2 7 1.3 16 1.4 18 1.5 21 1.6 23 References 27 ХШ xiv CHAPTER Theoretical Description of NMR Spectroscopy 2.1 2.1.1 2.1.2 2.1.3 2.1.4 2.2 2.2.1 2.2.2 2.2.3 2.2.4 2.2.5 2.3 2.4 2.4.1 2.4.2 2.5 2.5.1 2.5.2 2.5.3 2.5.4 2.6 2.7 2.7.1 2.7.2 2.7.3 2.7.3.1 2.7.3.2 2.7.3.3 2.7.4 Operators 2.7.5 2.7.6 Multiple-Quantum Coherence Contents 2.7.7 2.7.7.1 2.7.7.2 Transfer 2.7.7.3 2.7.7.4 Transfer 2.8 Interactions References CHAPTER Experimental Aspects of NMR Spectroscopy 3.1 114 3.2 124 3.2.1 124 3.2.2 126 3.2.3 132 3.3 136 3.3.1 136 3.3.2 142 3.3.2.1 142 3.3.2.2 143 3.3.2.3 151 3.3.3 158 3.3.4 159 3.3.4.1 160 3.3.4.2 161 3.4 165 3.4.1 165 3.4.2 172 3.4.3 174 3.4.4 179 3.4.5 181 3.4.6 189 XVI Contents 3.5 Spin Decoupling 201 3.5.1 201 3.5.2 204 3.5.3 209 3.5.4 212 3.5.5 216 3.6 Bo Field Gradients 217 3.7 Water Suppression Techniques 221 3.7.1 223 3.7.2 Sequences 224 3.7.3 227 3.7.4 232 3.8 One-Dimensional 234 3.8.1 234 3.8.2 236 3.8.2.1 236 3.8.2.2 237 3.8.2.3 238 3.8.2.4 252 3.8.2.5 257 3.8.2.6 259 3.8.3 262 3.8.4 263 3.8.4.1 263 3.8.4.2 Hahn 265 References 267 CH APTER Multidimensional NMR Spectroscopy 4.1 4.2 4.2.1 4.2.1.1 4.2.1.2 Contents 4.2.2 4.2.3 4.2.4 Coupling Hamiltonians 4.3 4.3.1 4.3.2 4.3.2.1 Pathway 4.3.2.2 4.3.2.3 4.3.2.4 4.3.3 4.3.3.1 Pathway 4.3.3.2 4.3.3.3 4.3.4 4.3.4.1 Cycling 4.3.4.2 Gradients 4.3.4.3 Multidimensional NMR Spectroscopy 4.4 4.5 References CHAPTER Relaxation and Dynamic Processes 5.1 5.1.1 5.1.2 5.1.3 5.1.4 xviii 5.2 5.2.1 5.2.2 Approximation 5.2.3 5.3 5.4 5.4.1 System 5.4.2 for Scalar-Coupled IS Spin System 5.4.3 System in the Rotating Frame 5.4.4 Relaxation 5.4.5 5.4.6 5.5 5.6 5.6.1 5.6.2 Scalar-Coupled Systems References CHAPTER Experimental lE NMR Methods 6.1 6.2 6.2.1 6.2.1.1 6.2.1.2 6.2.1.3 6.2.1.4 6.2.1.5 Constants in COSY Spectra Contents 6.2.1.6 6.2.2 6.2.2.1 6.2.2.2 6.2.2.3 6.2.2.4 6.2.3 6.3 6.3.1 6.3.1.1 6.3.1.2 6.3.1.3 6.3.1.4 6.3.2 6.3.2.1 6.3.2.2 6.3.2.3 6.3.3 6.3.3.1 6.3.3.2 6.3.3.3 6.3.3.4 6.3.3.5 6.4 6.4.1 6.4.1.1 6.4.1.2 6.4.1.3 6.4.1.4 6.4.2 6.4.2.1 6.4.2.2 6.4.2.3 6.5 6.5.1 6.5.2 6.5.3 xx 6.5.4 6.5.5 6.6 6.6.1 6.6.1.1 6.6.1.2 6.6.1.3 6.6.1.4 6.6.1.5 6.6.2 6.6.2.1 6.6.2.2 6.6.2.3 6.6.2.4 6.7 6.7.1 6.7.2 6.7.3 6.7.4 References CHAPTER Heteronuclear NMR Experiments 7.1 7.1.1 7.1.1.1 7.1.1.2 7.1.1.3 7.1.1.4 Spectra 7.1.2 Correlation Experiments 7.1.2.1 Suppression 7.1.2.2 Structure Contents 7.1.2.3 7.1.2.4 Experiments 7.1.3 TROSY Experiments 7.1.3.1 7.1.3.2 7.1.3.3 7.1.3.4 PEP-HSQC, and TROSY Experiments 7.1.3.5 Spectra of Larger Proteins 7.1.4 Heteronuclear Correlation Spectra 7.1.4.1 7.1.4.2 TROSY NMR Spectroscopy 7.1.5 7.2 7.2.1 3D 7.2.1.1 3D 7.2.1.2 3D 7.2.2 3D 7.2.3 3D Experiments 7.2.4 7.2.4.1 3D 7.2.4.2 7.2.4.3 7.2.4.4 Spectra 7.2.5 Heteronuclear-Edited NOESY Spectroscopy 7.3 HCCH-TOCSY Experiments 7.3.1 7.3.2 7.3.3 xxii 7.4 3D 7.4.1 HNCA 7.4.1.1 7.4.1.2 7.4.1.3 7.4.1.4 Experiment 7.4.1.5 Experiment 7.4.2 Experiment 7.4.3 H(CA)NH 7.4.4 7.4.4.1 7.4.4.2 7.4.5 7.4.5.1 7.4.5.2 7.4.5.3 7.4.6 Experiments 7.5 7.5.1 7.5.2 7.6 Constants References CHAPTER Experimental NMR Relaxation Methods 8.1 8.2 8.2.1 Relaxation Contents 8.2.2 Interference 8.2.3 Laboratory-Frame Relaxation 8.2.4 Relaxation 8.3 8.3.1 8.3.2 8.3.3 8.3.4 8.3.5 Spectroscopy 8.3.6 References CHAPTER Larger Proteins and Molecular Interactions 9.1 9.1.1 9.1.2 Random Fractionally Deuterated Proteins 9.1.3 9.1.4 9.1.5 Assignments in Deuterated Proteins 9.1.5.1 Proteins 9.1.5.2 9.1.5.3 Assignments 9.1.6 proteins 9.1.7 xxiv 9.1.8 9.1.8.1 Experiment 9.1.8.2 NOESY Experiments on Random Fractionally Deuterated Proteins 9.1.9 9.2 9.2.1 9.2.2 9.2.2.1 9.2.2.2 9.2.2.3 Solvent Exchange 9.2.3. Restraints for Protein Complexes 9.2.3.1 Protein-Ligand Complexes 9.2.3.2 Intermolecular Interfaces 9.3 9.3.1 9.3.2 9.3.3 References CHAPTER Sequential Assignment, Structure Determination, and Other Applications 10.1 10.1.1 Proteins 10.1.2 Isotopically Labeled Proteins 10.2 Contents 10.2.1 10.2.1.1 10.2.1.2 Scalar Coupling Constants 10.2.1.3 Chemical Shifts 10.2.1.4 Constants 10.2.1.5 Proton-Solvent Exchange 10.2.1.6 Trans-Hydrogen Bond Scalar Coupling Constants 10.2.2 10.3 References Table of Symbols List of Figures List of Tables Suggested Reading Index For the reader s easy reference, the Table of Constants and the Spin-1/2 Product Operator Equations are given on the inside back cover end pages.
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spellingShingle Protein NMR spectroscopy principles and practice
Nuclear magnetic resonance spectroscopy Laboratory manuals
Proteins Analysis Laboratory manuals
Proteine (DE-588)4076388-2 gnd
Chemische Analyse (DE-588)4009840-0 gnd
NMR-Spektroskopie (DE-588)4075421-2 gnd
subject_GND (DE-588)4076388-2
(DE-588)4009840-0
(DE-588)4075421-2
title Protein NMR spectroscopy principles and practice
title_auth Protein NMR spectroscopy principles and practice
title_exact_search Protein NMR spectroscopy principles and practice
title_full Protein NMR spectroscopy principles and practice John Cavanagh ...
title_fullStr Protein NMR spectroscopy principles and practice John Cavanagh ...
title_full_unstemmed Protein NMR spectroscopy principles and practice John Cavanagh ...
title_short Protein NMR spectroscopy
title_sort protein nmr spectroscopy principles and practice
title_sub principles and practice
topic Nuclear magnetic resonance spectroscopy Laboratory manuals
Proteins Analysis Laboratory manuals
Proteine (DE-588)4076388-2 gnd
Chemische Analyse (DE-588)4009840-0 gnd
NMR-Spektroskopie (DE-588)4075421-2 gnd
topic_facet Nuclear magnetic resonance spectroscopy Laboratory manuals
Proteins Analysis Laboratory manuals
Proteine
Chemische Analyse
NMR-Spektroskopie
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