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这是新版的，我买了一本纸版的是中文的。不过中文的没有脉冲程序，不容易看，也没有很多时间去看。
2 W$ X: O7 g. w( r; m , {. i- ?% M1 a5 _# ?4 q+ M5 |' ~
下面是网上的一些内容。 : t% L; V6 t# x- j
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200 and More NMR Experiments : A Practical Course
by Stefan Berger, Siegmar Braun 1 e; V1 H1 k, b. [' P. n2 g- i
Review
"This book is an excellent catalogue of useful NMR experiments for people who are looking for the most suitable experiment to solve a specific problem.
It collects in one place all the currently pulse sequences from liquid NMR spectroscopy, discusses their relative merits, the time required to perform them and gives experimental examples measured by the authors for this book. ... In conclusion, I think this book is a great encyclopedia of the techniques of modern liquid state NMR spectroscopy. It is highly readabele and should be on the shelf of any serious NMR spectroscopist, who does more complicated experiments than routine H-NMR spectroscopy. Finally instrument vendors should consider packing at least one copy of this book with every new NMR machine and using it as an educational toot when installing the machine." ! w2 J3 B2 K1 `: q* M& |' {* Y
Book Description
This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein:
· Which experiment can best yield the desired information?
· How must the chosen experiment be performed?
· How does one read the required information from the spectrum?
· How does this particular pulse sequence work?
· Which other experiments give similar information?
This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids.
What is new in this third edition?
1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS.
2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure.
The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses
From the Back Cover
This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein: , ^! v) H8 d% n2 @% Z
. f& ]' ~/ u ?" Z/ H6 H7 D- Which experiment can best yield the desired information?
/ Q6 N, L% x; M: _, J- How must the chosen experiment be performed?
! E' Q6 y6 H$ f+ t# N
- How does one read the required information from the spectrum?
, e/ r5 d U/ b# E; b' w
- How does this particular pulse sequence work?
% G3 u* [$ y6 ^4 B- Which other experiments give similar information?
5 v& |3 g7 P j7 x0 [This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids. 5 [. u; H1 v# p* S: L6 P
What is new in this third edition?
! y* p9 M+ j; {* j! S4 @1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS.
2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure.
" E# Q6 y M7 l2 }. y) bThe guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses. 3 T2 @0 s5 m5 t, V
Contents
* b( M1 j! d: i* X( @) T$ aPreface $ {: ~- I8 P6 R. c
Chapter 1 The NMR Spectrometer
5 }- e1 _9 L1 ?& a5 H1 }1 G7 Q: T1.1 Components of an NMR Spectrometer
1.1.1 The Magnet
1.1.2 The Spectrometer Cabinet
1.1.3 The Computer
1.1.4 Maintenance
1.2 Tuning a Probe-Head
1.3 The Lock Channel
1.4 The Art of Shimming
1.4.1 The Shim Gradients
1.4.2 The Shimming Procedure
1.4.3 Gradient Shimming
+ j8 ~! H: _2 U4 EChapter 2 Determination of Pulse-Duration # @' ?9 ~4 K( i. [7 o: T& ~' P: b2 l3 [
Exp. 2.1: Determination of the 90° 1H Transmitter Pulse-Duration
Exp. 2.2: Determination of the 90° 13C Transmitter Pulse-Duration
Exp. 2.3: Determination of the 90° 1H Decoupler Pulse-Duration
Exp. 2.4: The 90° 1H Pulse with Inverse Spectrometer Configuration
Exp. 2.5: The 90° 13C Decoupler Pulse with Inverse Configuration
Exp. 2.6: Composite Pulses
Exp. 2.7: Radiation Damping
Exp. 2.8: P ulse and Receiver Phases
Exp. 2.9: Determination of Radiofrequency Power
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Chapter 3 Routine NMR Spectroscopy and Standard Tests
1 y' M: U% z2 Q, f+ L2 ]3 x3 _7 p/ gExp. 3.1: The Standard 1H NMR Experiment
Exp. 3.2: The Standard 13C NMR Experiment
Exp. 3.3: The Application of Window Functions
Exp. 3.4: Computer-Aided Spectral Analysis
Exp. 3.5: Line Shape Test for 1H NMR Spectroscopy
Exp. 3.6: Resolution Test for 1H NMR Spectroscopy
Exp. 3.7: Sensitivity Test for 1H NMR Spectroscopy
Exp. 3.8: Line Shape Test for 13C NMR Spectroscopy
Exp. 3.9: ASTM Sensitivity Test for 13C NMR Spectroscopy
Exp. 3.10 :Sensitivity Test for 13C NMR Spectroscopy
Exp. 3.11: Quadrature Image Test
Exp. 3.12: Dynamic Range Test for Signal Amplitudes
Exp. 3.13: 13° Phase Stability Test
Exp. 3.14: Radiofrequency Field Homogeneity
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Chapter 4 Decoupling Techniques
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Exp. 4.1: Decoupler Calibration for Homonuclear Decoupling
Exp. 4.2: Decoupler Calibration for Heteronuclear Decoupling
Exp. 4.3: Low-Power Calibration for Heteronuclear Decoupling
Exp. 4.4: Homonuclear Decoupling
Exp. 4.5: Homonuclear Decoupling at Two Frequencies
Exp. 4.6: The Homonuclear SPT Experiment
Exp. 4.7: The Heteronuclear SPT Experiment
Exp. 4.8: The Basic Homonuclear NOE Difference Experiment
Exp. 4.9: 1D Nuclear Overhauser Difference Spectroscopy
Exp. 4.10: 1D NOE Spectroscopy with Multiple Selective Irradiation
Exp. 4.11: 1H Off-Resonance Decoupled 13C NMR Spectra
Exp. 4.12: The Gated 1H-Decoupling Technique
Exp. 4.13: The Inverse Gated 1H-Decoupling Technique
Exp. 4.14: 1H Single-Frequency Decoupling of 13C NMR Spectra
Exp. 4.15: 1H Low-Power Decoupling of 13C NMR Spectra
Exp. 4.16: Measurement of the Heteronuclear Overhauser Effect ; F7 Z+ Z }0 }, Q- o' C
Chapter 5 Dynamic NMR Spectroscopy
- z: x. q2 a G- ?/ KExp. 5.1: Low-Temperature Calibration Using Methanol
Exp. 5.2: High-Temperature Calibration Using 1,2-Ethanediol
Exp. 5.3: Dynamic 1H NMR Spectroscopy on Dimethylformamide
Exp. 5.4: The Saturation Transfer Experiment
Exp. 5.5: Measurement of the Rotating-Frame Relaxation Time T1
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Chapter 6 1D Multipulse Sequences
# C) k0 v+ j$ `5 ~2 dExp. 6.1: Measurement of the Spin Lattice Relaxation Time T1
Exp. 6.2: Measurement of the Spin Spin Relaxation Time T2
Exp. 6.3: 13C NMR Spectra with SEFT
Exp. 6.4: 13C NMR Spectra with APT
Exp. 6.5: The Basic INEPT Technique
Exp. 6.6: INEPT+
Exp. 6.7: Refocused INEPT
Exp. 6.8: Reverse INEPT
Exp. 6.9: DEPT-135
Exp. 6.10: Editing 13C NMR Spectra Using DEPT
Exp. 6.11: DEPTQ
Exp. 6.12: Multiplicity Determination Using PENDANT
Exp. 6.13: 1D-INADEQUATE
Exp. 6.14: The BIRD Filter
Exp. 6.15: TANGO
Exp. 6.16: The Heteronuclear Double-Quantum Filter
Exp. 6.17: Purging with a Spin-Lock Pulse
Exp. 6.18: Water Suppression by Presaturation
Exp. 6.19: Water Suppression by the Jump-and-Return Method
$ z" l2 k9 h9 I. Q9 lChapter 7 NMR Spectroscopy with Selective Pulses 1 K1 P" [' l4 s; p7 E
Exp. 7.1: Determination of a Shaped 90° 1H Transmitter Pulse
Exp. 7.2: Determination of a Shaped 90° 1H Decoupler Pulse
Exp. 7.3: Determination of a Shaped 90° 13C Decoupler Pulse
Exp. 7.4: Selective Excitation Using DANTE
Exp. 7.5: SELCOSY
Exp. 7.6: SELINCOR: Selective Inverse H,C Correlation via 1J(C,H)
Exp. 7.7: SELINQUATE
Exp. 7.8: Selective TOCSY
Exp. 7.9: INAPT
Exp. 7.10: Determination of Long-Range C,H Coupling Constants
Exp. 7.11: SELRESOLV
Exp. 7.12: SERF * ^$ d7 j, c: ^) Y& V8 U4 p7 r% o
Chapter 8 Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms
8 S t: b" U1 l! b0 a! U! r, d1 }
Exp. 8.1: Signal Separation Using a Lanthanide Shift Reagent
Exp. 8.2: Signal Separation of Enantiomers Using a Chiral Shift Reagent
Exp. 8.3: Signal Separation of Enantiomers Using a Chiral Solvating Agent
Exp. 8.4: Determination of Enantiomeric Purity with Pirkle's Reagent
Exp. 8.5: Determination of Enantiomeric Purity by 31P NMR
Exp. 8.6: Determination of Absolute Configuration by the Advanced Mosher Method
Exp. 8.7: Aromatic Solvent-Induced Shift (ASIS)
Exp. 8.8: NMR Spectroscopy of OH Protons and H/D Exchange
Exp. 8.9: Water Suppression Using an Exchange Reagent
Exp. 8.10: Isotope Effects on Chemical Shielding
Exp. 8.11: pKa Determination by 13C NMR
Exp. 8.12: Determination of Association Constants Ka
Exp. 8.13: Saturation Transfer Difference NMR
Exp. 8.14: The Relaxation Reagent Cr(acac)3
Exp. 8.15: Determination of Paramagnetic Susceptibility by NMR
Exp. 8.16: 1H and 13C NMR of Paramagnetic Compounds
Exp. 8.17: The CIDNP Effect
Exp. 8.18: Quantitative 1H NMR Spectroscopy: Determination of the Alcohol Content of Polish Vodka
Exp. 8.19: Quantitative 13C NMR Spectroscopy with Inverse Gated 1H-Decoupling
Exp. 8.20: NMR Using Liquid-Crystal Solvents ; l, n1 a* H" Y2 F
Chapter 9 Heteronuclear NMR Spectroscopy
! i; h5 r8 s5 ]+ o {8 E; XExp. 9.1: 1H-Decoupled 15N NMR Spectra Using DEPT
Exp. 9.2: 1H-Coupled 15N NMR Spectra Using DEPT
Exp. 9.3: 19F NMR Spectroscopy
Exp. 9.4: 29Si NMR Spectroscopy Using DEPT
Exp. 9.5: 29Si NMR Spectroscopy Using Spin-Lock Polarization
Exp. 9.6: 119Sn NMR Spectroscopy
Exp. 9.7: 2H NMR Spectroscopy
Exp. 9.8: 11B NMR Spectroscopy
Exp. 9.9: 17O NMR Spectroscopy Using RIDE
Exp. 9.10: 47/49Ti NMR Spectroscopy Using ARING
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Chapter 10 The Second Dimension
3 t& I6 y. @9 d' KExp. 10.1: 2D J-Resolved 1H NMR Spectroscopy
Exp. 10.2: 2D J-Resolved 13C NMR Spectroscopy
Exp. 10.3: The Basic H,H-COSY Experiment
Exp. 10.4: Long-Range COSY
Exp. 10.5: Phase-Sensitive COSY
Exp. 10.6: Phase-Sensitive COSY-45
Exp. 10.7: E.COSY
Exp. 10.8: Double-Quantum-Filtered COSY with Presaturation
Exp. 10.9: Fully Coupled C,H Correlation (FUCOUP)
Exp. 10.10: C,H-Correlation by Polarization Transfer (HETCOR)
Exp. 10.11: Long-Range C,H-Correlation by Polarization Transfer
Exp. 10.12: C,H Correlation via Long-Range Couplings (COLOC)
Exp. 10.13: The Basic HMQC Experiment
Exp. 10.14: Phase-Sensitive HMQC with BIRD Filter and GARP Decoupling
Exp. 10.15: Poor Man's Gradient HMQC
Exp. 10.16: Phase-Sensitive HMBC with BIRD Filter
Exp. 10.17: The Basic HSQC Experiment
Exp. 10.18: The HOHAHA or TOCSY Experiment
Exp. 10.19: HETLOC
Exp. 10.20: The NOESY Experiment
Exp. 10.21: The CAMELSPIN or ROESY Experiment
Exp. 10.22: The HOESY Experiment
Exp. 10.23: 2D-INADEQUATE
Exp. 10.24: The EXSY Experiment
Exp. 10.25: X,Y-Correlation
, O4 M. |% j! d, U2 HChapter 11 1D NMR Spectroscopy with Pulsed Field Gradients , u7 s1 [$ D3 h% L
Exp. 11.1: Calibration of Pulsed Field Gradients
Exp. 11.2: Gradient Pre-emphasis
Exp. 11.3: Gradient Amplifier Test
Exp. 11.4: Determination of Pulsed Field Gradient Ring-Down Delays
Exp. 11.5: The Pulsed Field Gradient Spin-Echo Experiment
Exp. 11.6: Excitation Pattern of Selective Pulses
Exp. 11.7: The Gradient Heteronuclear Double-Quantum Filter
Exp. 11.8: The Gradient zz-Filter
Exp. 11.9: The Gradient-Selected Dual Step Low-Pass Filter
Exp. 11.10: gs-SELCOSY
Exp. 11.11: gs-SELTOCSY
Exp. 11.12: DPFGSE-NOE
Exp. 11.13: gs-SELINCOR
Exp. 11.14: SELINCOR-TOCSY
Exp. 11.15: GRECCO
Exp. 11.16: WATERGATE
Exp. 11.17: Water Suppression by Excitation Sculpting
Exp. 11.18: Solvent Suppression Using WET
Exp. 11.19: DOSY
Exp. 11.20: INEPT-DOSY
Exp. 11.21: DOSY-HMQC
. I M/ ^- ] E. }$ i
Chapter 12 2D NMR Spectroscopy With Field Gradients
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Exp. 12.1: gs-COSY
Exp. 12.2: Constant-Time COSY
Exp. 12.3: Phase-Sensitive gs-DQF-COSY
Exp. 12.4: gs-HMQC
Exp. 12.5: gs-HMBC
Exp. 12.6: ACCORD-HMBC
Exp. 12.7: HMSC
Exp. 12.8: Phase-Sensititive gs-HSQC with Sensitivity Enhancement
Exp. 12.9: Edited HSQC with Sensitivity Enhancement
Exp. 12.10: HSQC with Adiabatic Pulses for High-Field Instruments
Exp. 12.11: gs-TOCSY
Exp. 12.12: gs-HMQC-TOCSY
Exp. 12.13: gs-HETLOC
Exp. 12.14: gs-J-Resolved HMBC
Exp. 12.15: 2Q-HMBC
Exp. 12.16: 1H-Detected 2D INEPT-INADEQUATE
Exp. 12.17: 1,1-ADEQUATE
Exp. 12.18: 1,n-ADEQUATE
Exp. 12.19: gs-NOESY
Exp. 12.20: gs-HSQC-NOESY
Exp. 12.21: gs-HOESY
Exp. 12.22: 1H,15N Correlation with gs-HMQC & v1 ]7 P! B/ G& |# K0 L8 I
Chapter 13 The Third Dimension
0 N8 q9 C) }; EExp. 13.1: 3D HMQC-COSY
Exp. 13.2: 3D gs-HSQC-TOCSY
Exp. 13.3: 3D H,C,P-Correlation
Exp. 13.4: 3D HMBC ) V; V" L4 [% Y: l; h3 t
Chapter 14 Solid-State NMR Spectroscopy
* D/ U4 y0 U% Q. ]1 X4 u0 a5 pExp. 14.1: Shimming Solid-State Probe-Heads
Exp. 14.2: Adjusting the Magic Angle
Exp. 14.3: Hartmann Hahn Matching
Exp. 14.4: The Basic CP/MAS Experiment
Exp. 14.5: TOSS
Exp. 14.6: SELTICS
Exp. 14.7: Connectivity Determination in the Solid State
Exp. 14.8: REDOR
Exp. 14.9: High-Resolution Magic-Angle Spinning
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Chapter 15 Protein NMR
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Exp. 15.1: Pulse Determination for Protein NMR
Exp. 15.2: HN-HSQC
Exp. 15.3: HC-HSQC
Exp. 15.4: MUSIC
Exp. 15.5: HN-Correlation using TROSY
Exp. 15.6: HN-TOCSY-HSQC
Exp. 15.7: HNCA
Exp. 15.8: HN(CO)CA
Exp. 15.9: HNCO
Exp. 15.10: HN(CA)CO
Exp. 15.11: HCACO
Exp. 15.12: HCCH-TOCSY
Exp. 15.13: CBCANH
Exp. 15.14: CBCA(CO)NH
Exp. 15.15: HBHA(CBCACO)NH
Exp. 15.16: HN(CA)NNH
Exp. 15.17: HN-NOESY-HSQC
Exp. 15.18: HC-NOESY-HSQC
Exp. 15.19: 3D HCN-NOESY
Exp. 15.20: HNCA-J
2 Z+ r0 c$ B6 X6 B9 ~0 uAppendix 1
Pulse Programs
; g6 p7 V9 h5 t UAppendix 2
Instrument Dialects
! p& o7 y' w- M- ]0 Z3 fAppendix 3
Classification of Experiments
/ T- f$ U# z' l! @0 Z: ?Appendix 4
Elementary Product Operator Formalism Rules
7 q! a0 W% X# Y/ H% C8 ~Appendix 5
Chemical Shift and Spin-Coupling Data for Ethyl Crotonate and Strychnine 5 [. F; N1 \, |8 W2 G
Glossary and Index
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发表于 2009-9-4 09:03:26
