Protein NMR spectroscopy: principles and practice
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Amsterdam [u.a.]
Academic Press
2007
|
| Ausgabe: | 2. ed. |
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XXV, 885 S. graph. Darst. |
| ISBN: | 9780121644918 012164491X |
Internformat
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| 245 | 1 | 0 | |a Protein NMR spectroscopy |b principles and practice |c John Cavanagh ... |
| 250 | |a 2. ed. | ||
| 264 | 1 | |a Amsterdam [u.a.] |b Academic Press |c 2007 | |
| 300 | |a XXV, 885 S. |b graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 4 | |a Nuclear magnetic resonance spectroscopy |v Laboratory manuals | |
| 650 | 4 | |a Proteins |x Analysis |v Laboratory manuals | |
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Datensatz im Suchindex
| _version_ | 1804132747467292672 |
|---|---|
| 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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| indexdate | 2024-07-09T19:57:44Z |
| institution | BVB |
| isbn | 9780121644918 012164491X |
| language | English |
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| physical | XXV, 885 S. graph. Darst. |
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| spelling | Protein NMR spectroscopy principles and practice John Cavanagh ... 2. ed. Amsterdam [u.a.] Academic Press 2007 XXV, 885 S. graph. Darst. txt rdacontent n rdamedia nc rdacarrier Nuclear magnetic resonance spectroscopy Laboratory manuals Proteins Analysis Laboratory manuals Proteine (DE-588)4076388-2 gnd rswk-swf Chemische Analyse (DE-588)4009840-0 gnd rswk-swf NMR-Spektroskopie (DE-588)4075421-2 gnd rswk-swf Proteine (DE-588)4076388-2 s Chemische Analyse (DE-588)4009840-0 s NMR-Spektroskopie (DE-588)4075421-2 s 1\p DE-604 Cavanagh, John Sonstige oth Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=012793980&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| 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 |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=012793980&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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