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第25楼2005/05/13
200个NMR实验:
200 and More NMR Experiments : A Practical Course
by Stefan Berger, Siegmar Braun
相关附件
200 and More NMR Experiments : A Practical Course
by Stefan Berger, Siegmar Braun
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."
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:
· 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.
Contents
Preface
Chapter 1 The NMR Spectrometer
1.1 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
Chapter 2 Determination of Pulse-Duration
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
Chapter 3 Routine NMR Spectroscopy and Standard Tests
Exp. 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. 3.1
