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    1. Naturvetenskap och teknik
    2. Matematik och naturvetenskap
    3. Kemi

    200 and More NMR Experiments

    A Practical Course

    AvStefan Berger,Siegmar Braun

    Häftad, Engelska, 2004

    1 108 kr

    Skickas . Fri frakt över 249 kr.

    Beskrivning

    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

    Produktinformation

    • Utgivningsdatum:2004-06-11
    • Mått:165 x 239 x 38 mm
    • Vikt:1 588 g
    • Format:Häftad
    • Språk:Engelska
    • Antal sidor:854
    • Upplaga:98002
    • Förlag:Wiley-VCH Verlag GmbH
    • ISBN:9783527310678

    Utforska kategorier

    • Kemi inom Naturvetenskap och teknik

    Mer om författaren

    Stefan Berger was intrigued by NMR after having won a bottle of beer during an introductory course in organic NMR led by Professor H. Suhr at the University of Tübingen in 1968. After completing a PhD thesis with Professor Anton Rieker, in 1973 he joined Professor J. D. Roberts at Caltech for postdoctoral work, where he also met Professor D.M. Grant and Professor D. Seebach, who were then guest professors in Pasadena. This period was decisive to try a Habilitation in NMR spectroscopy, which was achieved at the University Marburg. At the University Leipzig his aim is to combine methodological development of NMR and its application to bioorganic problems.

    Recensioner i media

    "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." Dr. Gerd Buntkowsky, FSU Jena, Zeitschrift fur Physikalische Chemie, Band 218, Heft 11 "This third edition serves as a detailed guide to NMR, complete with 206 experiments ranging form 1-D trials to more complex 3-D experiments on proteins." Analytical Chemistry, November 1, 2004 "The handbook is written by experts and gives very detailed step-by-step instructions. ... This excellent book is very well written and builds on the success of the earlier version that was largely due to its clarity, information content and the fact that the methods worked."J. Lindon, Chromatographia 2005, Vol. 61/No. 1/2 "I highly recommend this book to all scientists who are trying to implement new experimental schemes in liquid-state NMR spectroscopy. It is a very useful NMR >cookbook

    Innehållsförteckning

    • Preface vChapter 1 The NMR Spectrometer 11.1 Components of an NMR Spectrometer 11.1.1 The Magnet 11.1.2 The Spectrometer Cabinet 21.1.3 The Computer 31.1.4 Maintenance 31.2 Tuning a Probe-Head 31.3 The Lock Channel 41.4 The Art of Shimming 61.4.1 The Shim Gradients 61.4.2 The Shimming Procedure 81.4.3 Gradient Shimming 11Chapter 2 Determination of Pulse-Duration 14Exp. 2.1: Determination of the 90° 1H Transmitter Pulse-Duration 15Exp. 2.2: Determination of the 90° 13C Transmitter Pulse-Duration 18Exp. 2.3: Determination of the 90° 1H Decoupler Pulse-Duration 21Exp. 2.4: The 90° 1H Pulse with Inverse Spectrometer Configuration 24Exp. 2.5: The 90° 13C Decoupler Pulse with Inverse Configuration 27Exp. 2.6: Composite Pulses 30Exp. 2.7: Radiation Damping 33Exp. 2.8: Pulse and Receiver Phases 36Exp. 2.9: Determination of Radiofrequency Power 39Chapter 3 Routine NMR Spectroscopy and Standard Tests 43Exp. 3.1: The Standard 1H NMR Experiment 44Exp. 3.2: The Standard 13C NMR Experiment 49Exp. 3.3: The Application of Window Functions 54Exp. 3.4: Computer-Aided Spectral Analysis 58Exp. 3.5: Line Shape Test for 1H NMR Spectroscopy 61Exp. 3.6: Resolution Test for 1H NMR Spectroscopy 64Exp. 3.7: Sensitivity Test for 1H NMR Spectroscopy 67Exp. 3.8: Line Shape Test for 13C NMR Spectroscopy 70Exp. 3.9: ASTM Sensitivity Test for 13C NMR Spectroscopy 73Exp. 3.10: Sensitivity Test for 13C NMR Spectroscopy 76Exp. 3.11: Quadrature Image Test 79Exp. 3.12: Dynamic Range Test for Signal Amplitudes 82Exp. 3.13: 13° Phase Stability Test 85Exp. 3.14: Radiofrequency Field Homogeneity 88Chapter 4 Decoupling Techniques 91Exp. 4.1: Decoupler Calibration for Homonuclear Decoupling 92Exp. 4.2: Decoupler Calibration for Heteronuclear Decoupling 95Exp. 4.3: Low-Power Calibration for Heteronuclear Decoupling 98Exp. 4.4: Homonuclear Decoupling 101Exp. 4.5: Homonuclear Decoupling at Two Frequencies 104Exp. 4.6: The Homonuclear SPT Experiment 107Exp. 4.7: The Heteronuclear SPT Experiment 110Exp. 4.8: The Basic Homonuclear NOE Difference Experiment 113Exp. 4.9: 1D Nuclear Overhauser Difference Spectroscopy 116Exp. 4.10: 1D NOE Spectroscopy with Multiple Selective Irradiation 119Exp. 4.11: 1H Off-Resonance Decoupled 13C NMR Spectra 122Exp. 4.12: The Gated 1H-Decoupling Technique 125Exp. 4.13: The Inverse Gated 1H-Decoupling Technique 128Exp. 4.14: 1H Single-Frequency Decoupling of 13C NMR Spectra 131Exp. 4.15: 1H Low-Power Decoupling of 13C NMR Spectra 134Exp. 4.16: Measurement of the Heteronuclear Overhauser Effect 137Chapter 5 Dynamic NMR Spectroscopy 140Exp. 5.1: Low-Temperature Calibration Using Methanol 141Exp. 5.2: High-Temperature Calibration Using 1,2-Ethanediol 145Exp. 5.3: Dynamic 1H NMR Spectroscopy on Dimethylformamide 149Exp. 5.4: The Saturation Transfer Experiment 152Exp. 5.5: Measurement of the Rotating-Frame Relaxation Time T1ρ 155Chapter 6 1D Multipulse Sequences 159Exp. 6.1: Measurement of the Spin−Lattice Relaxation Time T1 160Exp. 6.2: Measurement of the Spin−Spin Relaxation Time T2 164Exp. 6.3: 13C NMR Spectra with SEFT 167Exp. 6.4: 13C NMR Spectra with APT 170Exp. 6.5: The Basic INEPT Technique 173Exp. 6.6: INEPT+ 176Exp. 6.7: Refocused INEPT 179Exp. 6.8: Reverse INEPT 182Exp. 6.9: DEPT-135 185Exp. 6.10: Editing 13C NMR Spectra Using DEPT 188Exp. 6.11: DEPTQ 191Exp. 6.12: Multiplicity Determination Using PENDANT 194Exp. 6.13: 1D-INADEQUATE 197Exp. 6.14: The BIRD Filter 201Exp. 6.15: TANGO 204Exp. 6.16: The Heteronuclear Double-Quantum Filter 207Exp. 6.17: Purging with a Spin-Lock Pulse 210Exp. 6.18: Water Suppression by Presaturation 213Exp. 6.19: Water Suppression by the Jump-and-Return Method 216Chapter 7 NMR Spectroscopy with Selective Pulses 219Exp. 7.1: Determination of a Shaped 90° 1H Transmitter Pulse 220Exp. 7.2: Determination of a Shaped 90° 1H Decoupler Pulse 223Exp. 7.3: Determination of a Shaped 90° 13C Decoupler Pulse 226Exp. 7.4: Selective Excitation Using DANTE 229Exp. 7.5: SELCOSY 232Exp. 7.6: SELINCOR: Selective Inverse H,C Correlation via 1J(C,H) 235Exp. 7.7: SELINQUATE 238Exp. 7.8: Selective TOCSY 242Exp. 7.9: INAPT 246Exp. 7.10: Determination of Long-Range C,H Coupling Constants 249Exp. 7.11: SELRESOLV 252Exp. 7.12: SERF 255Chapter 8 Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms 258Exp. 8.1: Signal Separation Using a Lanthanide Shift Reagent 259Exp. 8.2: Signal Separation of Enantiomers Using a Chiral Shift Reagent 262Exp. 8.3: Signal Separation of Enantiomers Using a Chiral Solvating Agent 265Exp. 8.4: Determination of Enantiomeric Purity with Pirkle’s Reagent 268Exp. 8.5: Determination of Enantiomeric Purity by 31P NMR 271Exp. 8.6: Determination of Absolute Configuration by the Advanced Mosher Method 274Exp. 8.7: Aromatic Solvent-Induced Shift (ASIS) 277Exp. 8.8: NMR Spectroscopy of OH Protons and H/D Exchange 280Exp. 8.9: Water Suppression Using an Exchange Reagent 283Exp. 8.10: Isotope Effects on Chemical Shielding 286Exp. 8.11: pKa Determination by 13C NMR 290Exp. 8.12: Determination of Association Constants Ka 293Exp. 8.13: Saturation Transfer Difference NMR 298Exp. 8.14: The Relaxation Reagent Cr(acac)3 302Exp. 8.15: Determination of Paramagnetic Susceptibility by NMR 305Exp. 8.16: 1H and 13C NMR of Paramagnetic Compounds 308Exp. 8.17: The CIDNP Effect 312Exp. 8.18: Quantitative 1H NMR Spectroscopy: Determination of the Alcohol Content of Polish Vodka 315Exp. 8.19: Quantitative 13C NMR Spectroscopy with Inverse Gated 1H-Decoupling 318Exp. 8.20: NMR Using Liquid-Crystal Solvents 321Chapter 9 Heteronuclear NMR Spectroscopy 324Exp. 9.1: 1H-Decoupled 15N NMR Spectra Using DEPT 330Exp. 9.2: 1H-Coupled 15N NMR Spectra Using DEPT 333Exp. 9.3: 19F NMR Spectroscopy 336Exp. 9.4: 29Si NMR Spectroscopy Using DEPT 339Exp. 9.5: 29Si NMR Spectroscopy Using Spin-Lock Polarization 342Exp. 9.6: 119Sn NMR Spectroscopy 346Exp. 9.7: 2H NMR Spectroscopy 349Exp. 9.8: 11B NMR Spectroscopy 352Exp. 9.9: 17O NMR Spectroscopy Using RIDE 355Exp. 9.10: 47/49Ti NMR Spectroscopy Using ARING 358Chapter 10 The Second Dimension 362Exp. 10.1: 2D J-Resolved 1H NMR Spectroscopy 367Exp. 10.2: 2D J-Resolved 13C NMR Spectroscopy 370Exp. 10.3: The Basic H,H-COSY Experiment 373Exp. 10.4: Long-Range COSY 377Exp. 10.5: Phase-Sensitive COSY 380Exp. 10.6: Phase-Sensitive COSY-45 383Exp. 10.7: E.COSY 386Exp. 10.8: Double-Quantum-Filtered COSY with Presaturation 389Exp. 10.9: Fully Coupled C,H Correlation (FUCOUP) 393Exp. 10.10: C,H-Correlation by Polarization Transfer (HETCOR) 396Exp. 10.11: Long-Range C,H-Correlation by Polarization Transfer 399Exp. 10.12: C,H Correlation via Long-Range Couplings (COLOC) 402Exp. 10.13: The Basic HMQC Experiment 405Exp. 10.14: Phase-Sensitive HMQC with BIRD Filter and GARP Decoupling 409Exp. 10.15: Poor Man’s Gradient HMQC 412Exp. 10.16: Phase-Sensitive HMBC with BIRD Filter 415Exp. 10.17: The Basic HSQC Experiment 418Exp. 10.18: The HOHAHA or TOCSY Experiment 422Exp. 10.19: HETLOC 426Exp. 10.20: The NOESY Experiment 430Exp. 10.21: The CAMELSPIN or ROESY Experiment 434Exp. 10.22: The HOESY Experiment 438Exp. 10.23: 2D-INADEQUATE 441Exp. 10.24: The EXSY Experiment 445Exp. 10.25: X,Y-Correlation 448Chapter 11 1D NMR Spectroscopy with Pulsed Field Gradients 453Exp. 11.1: Calibration of Pulsed Field Gradients 455Exp. 11.2: Gradient Pre-emphasis 458Exp. 11.3: Gradient Amplifier Test 461Exp. 11.4: Determination of Pulsed Field Gradient Ring-Down Delays 464Exp. 11.5: The Pulsed Field Gradient Spin-Echo Experiment 467Exp. 11.6: Excitation Pattern of Selective Pulses 470Exp. 11.7: The Gradient Heteronuclear Double-Quantum Filter 474Exp. 11.8: The Gradient zz-Filter 477Exp. 11.9: The Gradient-Selected Dual Step Low-Pass Filter 480Exp. 11.10: gs-SELCOSY 484Exp. 11.11: gs-SELTOCSY 488Exp. 11.12: DPFGSE-NOE 492Exp. 11.13: gs-SELINCOR 496Exp. 11.14: α/β-SELINCOR-TOCSY 499Exp. 11.15: GRECCO 503Exp. 11.16: WATERGATE 506Exp. 11.17: Water Suppression by Excitation Sculpting 509Exp. 11.18: Solvent Suppression Using WET 512Exp. 11.19: DOSY 515Exp. 11.20: INEPT-DOSY 518Exp. 11.21: DOSY-HMQC 521Chapter 12 2D NMR Spectroscopy With Field Gradients 525Exp. 12.1: gs-COSY 526Exp. 12.2: Constant-Time COSY 530Exp. 12.3: Phase-Sensitive gs-DQF-COSY 534Exp. 12.4: gs-HMQC 538Exp. 12.5: gs-HMBC 542Exp. 12.6: ACCORD-HMBC 546Exp. 12.7: HMSC 550Exp. 12.8: Phase-Sensititive gs-HSQC with Sensitivity Enhancement 554Exp. 12.9: Edited HSQC with Sensitivity Enhancement 558Exp. 12.10: HSQC with Adiabatic Pulses for High-Field Instruments 563Exp. 12.11: gs-TOCSY 567Exp. 12.12: gs-HMQC-TOCSY 571Exp. 12.13: gs-HETLOC 575Exp. 12.14: gs-J-Resolved HMBC 581Exp. 12.15: 2Q-HMBC 585Exp. 12.16: 1H-Detected 2D INEPT-INADEQUATE 589Exp. 12.17: 1,1-ADEQUATE 593Exp. 12.18: 1,n-ADEQUATE 597Exp. 12.19: gs-NOESY 601Exp. 12.20: gs-HSQC-NOESY 604Exp. 12.21: gs-HOESY 608Exp. 12.22: 1H,15N Correlation with gs-HMQC 612Chapter 13 The Third Dimension 616Exp. 13.1: 3D HMQC-COSY 618Exp. 13.2: 3D gs-HSQC-TOCSY 622Exp. 13.3: 3D H,C,P-Correlation 626Exp. 13.4: 3D HMBC 630Chapter 14 Solid-State NMR Spectroscopy 634Exp. 14.1: Shimming Solid-State Probe-Heads 635Exp. 14.2: Adjusting the Magic Angle 639Exp. 14.3: Hartmann−Hahn Matching 642Exp. 14.4: The Basic CP/MAS Experiment 645Exp. 14.5: TOSS 649Exp. 14.6: SELTICS 653Exp. 14.7: Connectivity Determination in the Solid State 656Exp. 14.8: REDOR 659Exp. 14.9: High-Resolution Magic-Angle Spinning 663Chapter 15 Protein NMR 666Exp. 15.1: Pulse Determination for Protein NMR 670Exp. 15.2: HN-HSQC 673Exp. 15.3: HC-HSQC 678Exp. 15.4: MUSIC 682Exp. 15.5: HN-Correlation using TROSY 688Exp. 15.6: HN-TOCSY-HSQC 692Exp. 15.7: HNCA 698Exp. 15.8: HN(CO)CA 705Exp. 15.9: HNCO 711Exp. 15.10: HN(CA)CO 718Exp. 15.11: HCACO 725Exp. 15.12: HCCH-TOCSY 732Exp. 15.13: CBCANH 739Exp. 15.14: CBCA(CO)NH 746Exp. 15.15: HBHA(CBCACO)NH 753Exp. 15.16: HN(CA)NNH 760Exp. 15.17: HN-NOESY-HSQC 766Exp. 15.18: HC-NOESY-HSQC 773Exp. 15.19: 3D HCN-NOESY 779Exp. 15.20: HNCA-J 785Appendix 1 791Pulse ProgramsAppendix 2 794Instrument DialectsAppendix 3 797Classification of ExperimentsAppendix 4 799Elementary Product Operator Formalism RulesAppendix 5 802Chemical Shift and Spin-Coupling Data for Ethyl Crotonate and StrychnineGlossary and Index 804