| 查看: 445 | 回复: 4 | |||
| 当前主题已经存档。 | |||
kingwin625木虫 (正式写手)
|
[交流]
【交流】关于“150 Basic NMR Experiments”附纳米盘上传地址
|
||
|
英文版的。 http://www.namipan.com/d/05%ef%b ... 8fd71512977e4a00700 前面的一些是对的，但后面有很多实验的信息是错的。特别是固体部分好像都不对。 我正在看这本书，大家可以交流一下。 |
回复此楼» 猜你喜欢
国自然申请面上模板最新2026版出了吗？
已经有10人回复
-
推荐一本书
已经有12人回复
-
基金申报
已经有4人回复
-
计算机、0854电子信息（085401-058412）调剂
已经有4人回复
-
溴的反应液脱色
已经有6人回复
-
纳米粒子粒径的测量
已经有7人回复
-
常年博士招收(双一流，工科)
已经有4人回复
-
参与限项
已经有5人回复
-
有没有人能给点建议
已经有5人回复
-
萌生出自己或许不适合搞科研的想法，现在跑or等等看？
已经有4人回复
» 本主题相关商家推荐: (我也要在这里推广)
kingwin625
木虫 (正式写手)
- 应助: 6 (幼儿园)
- 金币: 3953.6
- 红花: 1
- 帖子: 378
- 在线: 199小时
- 虫号: 521143
- 注册: 2008-03-08
- 专业: 分析仪器与试剂
|
下面是网上找的新版的，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，很多看不懂。也没有很多时间去看。希望和大家交流一下。 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. 3.14: Radiofrequency Field Homogeneity Chapter 4 Decoupling Techniques 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 Chapter 5 Dynamic NMR Spectroscopy Exp. 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 Chapter 6 1D Multipulse Sequences Exp. 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 Chapter 7 NMR Spectroscopy with Selective Pulses 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 Chapter 8 Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms 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 |
2楼2009-09-04 09:24:15
kingwin625
木虫 (正式写手)
- 应助: 6 (幼儿园)
- 金币: 3953.6
- 红花: 1
- 帖子: 378
- 在线: 199小时
- 虫号: 521143
- 注册: 2008-03-08
- 专业: 分析仪器与试剂
|
Chapter 9 Heteronuclear NMR Spectroscopy Exp. 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 Chapter 10 The Second Dimension Exp. 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 Chapter 11 1D NMR Spectroscopy with Pulsed Field Gradients 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 Chapter 12 2D NMR Spectroscopy With Field Gradients 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 Chapter 13 The Third Dimension Exp. 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 Chapter 14 Solid-State NMR Spectroscopy Exp. 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 Chapter 15 Protein NMR 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 Appendix 1 Pulse Programs Appendix 2 Instrument Dialects Appendix 3 Classification of Experiments Appendix 4 Elementary Product Operator Formalism Rules Appendix 5 Chemical Shift and Spin-Coupling Data for Ethyl Crotonate and Strychnine Glossary and Index |
3楼2009-09-04 09:25:52
|
本帖内容被屏蔽 |
4楼2009-09-04 12:55:44
kingwin625
木虫 (正式写手)
- 应助: 6 (幼儿园)
- 金币: 3953.6
- 红花: 1
- 帖子: 378
- 在线: 199小时
- 虫号: 521143
- 注册: 2008-03-08
- 专业: 分析仪器与试剂
5楼2009-09-04 13:36:58