Protein NMR Spectroscopy: Principles and Practice

Couverture
Academic Press, 1996 - 587 pages
Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy: Principles and Practice develops the complete repertoire of theoretical principals and experimental practices necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy: Principles and Practice is written as a graduate-level textbook and will be of particular interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or who wish to remain abreast of the latest developments in this increasingly important area.

* Special Features:
* First book to combine detailed NMR theory discussions with experimental applications to biomolecules.
* All the theory required to understand these experiments and others.
* Easy to follow progression from a fundamental level to an advanced level.
* Theory of NMR and practical applications for biomolecular investigations presented.
* Theory applied to very practical situations.
* Comprehensive treatment of different "levels" of theory from simple ideas to density matrix analysis and operator practices.
* Comprehensive description of multi dimensional NMR experiments as applied to unlabeled, 15N-labeled and doubly (13C/15N) labeled proteins.
 

Pages sélectionnées

Table des matières

11 Nuclear Magnetism
2
12 The Bloch Equations
6
13 The OnePulse NMR Experiment
14
14 Linewidth
16
15 Chemical Shift
19
16 Scalar Coupling and Limitations of the Bloch Equations
20
References
24
21 Postulates of Quantum Mechanics
25
521 INTERFERENCE EFFECTS
262
522 LIKE AND UNLIKE SPINS
263
523 RELAXATION IN THE ROTATING FRAME
264
53 Spectral Density Functions
265
54 Relaxation Mechanisms
270
541 INTRAMOLECULAR DIPOLAR RELAXATION FOR IS SPIN SYSTEM
271
542 INTRAMOLECULAR DIPOLAR RELAXATION FOR SCALAR COUPLED IS SPIN SYSTEM
279
543 INTRAMOLECULAR DIPOLAR RELAXATION FOR IS SPIN SYSTEM IN THE ROTATING FRAME
282

211 THE SCHRODINGER EQUATION
26
212 EIGENVALUE EQUATIONS
27
213 SIMULTANEOUS EIGENFUNCTIONS
30
214 EXPECTATION VALUE OF THE MAGNETIC MOMENT
31
22 The Density Matrix
33
222 QUANTUM STATISTICAL MECHANICS
36
223 THE LIOUVILLEVON NEUMANN EQUATION
37
224 THE ROTATINGFRAME TRANSFORMATION
39
225 MATRIX REPRESENTATIONS OF THE SPIN OPERATORS
40
23 Pulses and Rotation Operators
44
24 Quantum Mechanical NMR Spectroscopy
49
241 EQUILIBRIUM AND OBSERVATION OPERATORS
50
242 THE ONEPULSE EXPERIMENT
51
25 Quantum Mechanics of Multispin Systems
53
252 SCALAR COUPLING HAMILTONIAN
56
253 ROTATIONS IN PRODUCT SPACES
61
254 ONEPULSE EXPERIMENT FOR A TWOSPIN SYSTEM
64
26 Coherence
67
27 Product Operator Formalism
73
272 BASIS OPERATORS
75
273 EVOLUTION IN THE PRODUCT OPERATOR FORMALISM
79
274 SINGLEQUANTUM COHERENCE AND OBSERVABLE OPERATORS
83
275 MULTIPLEQUANTUM COHERENCE
85
276 COHERENCE TRANSFER AND GENERATION OF MULTIPLEQUANTUM COHERENCE
87
References
93
31 NMR Instrumentation
95
32 Data Acquisition
100
II
101
322 QUADRATURE DETECTION
103
33 Data Processing
105
331 FOURIER TRANSFORMATION
107
332 DATA MANIPULATIONS
111
333 SlGNALTONOISE RATIO
124
334 ALTERNATIVES TO FOURIER TRANSFORMATION
126
341 OFFRESONANCE EFFECTS
131
342 COMPOSITE PULSES
137
343 SPIN DECOUPLING
141
344 SELECTIVE PULSES
144
35 WaterSuppression Techniques
146
351 PRESATURATION
150
352 JUMPRETURN AND BINOMIAL SEQUENCES
151
353 SPIN LOCK AND GRADIENT PULSES
153
354 POST ACQUISITION SIGNAL PROCESSING
158
361 SAMPLE PREPARATION
160
362 INSTRUMENT SETUP
162
363 REFERENCING
175
364 ACQUISITION AND DATA PROCESSING
177
References
180
III
183
41 TwoDimensional NMR Spectroscopy
185
42 Coherence Transfer and Mixing
191
421 THROUGHBOND COHERENCE TRANSFER
192
422 THROUGHSPACE COHERENCE TRANSFER
202
423 HETERONUCLEAR COHERENCE TRANSFER
203
431 COHERENCELEVEL DIAGRAMS
204
432 PHASE CYCLES
207
433 PULSED FIELD GRADIENTS
220
434 FREQUENCY DISCRIMINATION
227
44 Resolution and Sensitivity
236
45 Three and FourDimensional NMR Spectroscopy
237
References
240
IV
243
51 Introduction and Survey of Theoretical Approaches
244
511 RELAXATION IN THE BLOCH EQUATIONS
246
512 THE SOLOMON EQUATIONS
247
513 BLOCK WANGSNESS AND REDFIELD THEORY
255
544 CHEMICALSHIFT ANISOTROPY AND QUADRUPOLAR RELAXATION
284
545 SCALAR RELAXATION
285
55 Nuclear Overhauser Effect
287
56 ChemicalExchange Effects in NMR Spectroscopy
290
561 CHEMICAL EXCHANGE FOR ISOLATED SPINS
291
562 QUALITATIVE EFFECTS OF CHEMICAL EXCHANGE IN SCALARCOUPLED SYSTEMS
298
References
299
V
301
61 Assessment of the ID H Spectrum
302
62 COSYType Experiments
305
622 RELAYED COSY
322
623 DOUBLERELAYED COSY
327
63 MultipleQuantumFiltered COSY
329
631 2QFCOSY
331
632 3QFCOSY
338
633 ECOSY
343
64 MultipleQuantum Spectroscopy
351
641 2Q SPECTROSCOPY
353
642 3Q SPECTROSCOPY
367
65 TOCSY
371
651 PRODUCT OPERATOR ANALYSIS
372
VI
375
653 PROCESSING
378
654 INFORMATION CONTENT
379
655 EXPERIMENTAL VARIANTS
381
662 ROESY
394
67 H 3D Experiments
402
671 EXPERIMENTAL PROTOCOL
404
673 INFORMATION CONTENT
406
References
407
VII
410
71 Heteronuclear Correlation NMR Spectroscopy
411
711 BASIC HETERONUCLEAR CORRELATION EXPERIMENTS
413
712 ADDITIONAL CONSIDERATIONS IN HMQC AND HSQC EXPERIMENTS
423
713 VARIANT HSQC EXPERIMENTS
435
72 HeteronuclearEdited NMR Spectroscopy
447
722 3D TOCSYHSQC SPECTROSCOPY
453
723 3D HSQCNOESY AND HSQCTOCSY EXPERIMENTS
457
724 HMQCNOESYHMQC EXPERIMENTS
458
HETERONUCLEAREDITED NOESY SPECTROSCOPY
467
The HCCHCOSY and HCCHTOCSY Experiments
468
731 HCCHCOSY
469
732 CONSTANTTIME HCCHCOSY
473
733 HCCHTOCSY
475
74 3D TripleResonance Experiments
478
HNCA
482
THE HNCOCA EXPERIMENT
491
HCANH
495
744 OTHER TRIPLERESONANCE EXPERIMENTS FOR BACKBONE CORRELATIONS
499
745 CORRELATIONS WITH THE C3H3 SPINS
507
746 ADDITIONAL CONSIDERATIONS FOR TRIPLERESONANCE EXPERIMENTS
517
75 Measurement of Scalar Coupling Constants
518
751 HNCAJ EXPERIMENT
519
752 HNHA EXPERIMENT
524
References
528
VIII
532
81 Resonance Assignment Strategies
533
812 HETERONUCLEAR RESONANCE ASSIGNMENTS
541
82 ThreeDimensional Solution Structures
543
821 NMRDERIVED STRUCTURAL RESTRAINTS
545
822 STRUCTURE DETERMINATION
548
Beyond Structure
552
References
554
SUGGESTED READING
557
INDEX
559
Droits d'auteur

Autres éditions - Tout afficher

Protein NMR Spectroscopy: Principles and Practice
John Cavanagh,Wayne J. Fairbrother,Arthur G. Palmer, III,Nicholas J. Skelton
Aperçu limité - 1995
Protein NMR Spectroscopy: Principles and Practice
John Cavanagh,Nicholas J. Skelton,Wayne J. Fairbrother,Mark Rance,Arthur G. Palmer III
Aperçu limité - 2010

Expressions et termes fréquents

2QF-COSY 3JHH absorptive acquisition amide protons antiphase artifacts chemical shifts chemical-shift components composite pulse constant-time correlations COSY experiment coupling constants cross-peaks cross-relaxation D₂O decoupling delay density matrix density operator described dimension dipolar E-COSY effects equation evolution period F₁ F₂ F2 ppm FIGURE Fourier transformation frequency function Hamiltonian heteronuclear HMQC HNCA experiment homonuclear HSQC HSQC experiment in-phase increments intensity isotropic mixing Larmor frequency lineshape linewidth Magn magnetic field matrix mixing period multiple-quantum multiplet NMR experiments NMR spectroscopy NOESY nuclear nuclei observed obtained phase cycle product operator proteins protons pulse sequence pulsed field gradients quantum R. R. Ernst relaxation rate constants residues resonance rf field rf pulse ROESY S₂ sample scalar coupling constant scalar coupling interactions Section sequential shown in Fig signal solvent spectra spectral width spectrum spin system t₁ t₂ tion TOCSY transients transverse ubiquitin

Références à ce livre

À propos de l'auteur (1996)

Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at North Carolina State University. He is an expert in protein structural biology, particularly in how bacteria are able to protect themselves. Dr. Cavanagh received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of Structural Biology at the Wadsworth Center (New York State Department of Health), Associate Professor of Biomedical Sciences (SUNY) and Professor of Chemistry (Purdue). Since 2000 he has been Professor of Biochemistry in the Department of Molecular & Structural Biochemistry at North Carolina State University. Dr. Cavanagh has served on numerous NIH and NSF grant review panels and is currently a permanent member of the MSFB Study Section at NIH. He has authored over 100 peer-reviewed research publications and has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), the Fullsome Award (1996), the NC State University Alumni Associations Outstanding Research Award (2005) and Entrepreneur of the Year- NC State University (2012). He runs the Jimmy V-NCSU Cancer Therapeutics Training Program, was Assistant Vice Chancellor for Research at NC State from 2012-2014 and is the co-founder and Chief Scientific Officer of Agile Sciences Inc., a Raleigh based biotechnology company focusing on antibiotic resistance.

Informations bibliographiques

TitreProtein NMR Spectroscopy: Principles and Practice
AuteurJohn Cavanagh
Éditionillustrée, réimprimée
ÉditeurAcademic Press, 1996
ISBN0121644901, 9780121644901
Longueur587 pages
  
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