HMBC 17. Goto. Introduction AVANCE User s Guide Bruker 185

Similar documents
8 COSY. 8.1 Introduction. 8.2 Magnitude COSY

Two Dimensional Homonuclear Correlation Spectroscopy

Two Dimensional Homonuclear Correlation Spectroscopy

Two Dimensional Heteronuclear Correlation Spectroscopy

User manual Bruker DPX200 NMR spectrometer

400 MHz spectrometer user manual

2D heteronuclear correlation experiments

Implementing ultrafast 2D NMR experiments on a Bruker Avance Spectrometer

Chem 203 December 15, Final Exam Part II Problem 3 of 3 (30 points)

Chem 203 December 15, Final Exam Part II Problem 2 of 3 (30 points)

Fast Methods for Small Molecules

KJM D-SELECTIVE NMR Experiments on the AVIIIHD-800. Version 1.0. Topspin 3.5 Windows 7

Program. short intro the hardware locking and shimming 1D proton setup presaturation spectra

KJM D-SELECTIVE NMR Experiments on the AVI-600 and AVII-600. Version 1.0. Topspin 3.5 Windows 7 Topspin 1.3 Windows XP

Open acqi window if the button has been lost. autolocking routine, alock= y for autolocking, alock= n for typical manual locking

NMR Hardware 06/06/2017. Outline. Instrumentation: Magnet. Increasing magnetic field increases Sensitivity, by power of 3/2 Dispersion, linearly

Step by step procedure for NMR data acquisition

H Micro-Imaging. Tuning and Matching. i. Open any 1H data set and type wobb.

NMR Spectrometer Operation: xwinnmr

1D Transient NOE on the Bruker DRX-500 and DRX-600

PINMRF. Varian 300 MHz NMR Spectrometers User Guide for Advanced 1D and Basic 2D NMR Experiments

Ultrahigh-resolution Total Correlation NMR Spectroscopy

SUPPORTING INFORMATION

NMR spectrometer usage at the BioNMR facility ETH Zürich

Student Name: Date Completed: Supervisor:

TopSpin Guide Book. Basic NMR Experiments User Manual. Innovation with Integrity. Version 002 NMR

Eclipse+ NMR Training Guide

Laboratory Experiments for Nuclear Magnetic Resonance Spectroscopy May 6, 2004

Chem 203. Organic Spectroscopy. Midterm Examination, Part II (60 points total) Problem 4 of 4 (three out of four required, 20 points)

Instructions for 1 H-, 13 C-, 19 F-, and 31 P-Spectra on the Varian Mercury-Vx-300

Your first NMR measurement

Chem 203. Organic Spectroscopy. Midterm Examination, Part II (60 points total) Problem 1 of 4 (three out of four required, 20 points)

Chem 203. Organic Spectroscopy. Midterm Examination, Part II (60 points total) Problem 4 of 4 (three out of four required, 20 points)

NMR Basics. Lecture 2

If the magnetic field is larger, more energy is required to excite a given nucleus.

10. Phase Cycling and Pulsed Field Gradients Introduction to Phase Cycling - Quadrature images

An NMR Caveman s Guide to Quickly Acquiring Spectroscopic Data By Brian Sparling

NMR Spectroscopy with Radio Frequency Gradients.

GUIDELINES FOR THE REPRESENTATION OF PULSE SEQUENCES FOR SOLUTION-STATE NUCLEAR MAGNETIC RESONANCE SPECTROMETRY

Relaxation-encoded NMR experiments for mixture analysis: REST and beer. Electronic Supporting Information

Gradients. Effects of B0 gradients on transverse magnetisation Similar to figure 10 of Sattler review Progr. NMR 34 (1999), 93

CLIP-HSQMBC: Easy measurement of small proton-carbon coupling constants in organic molecules

Chapter 11 Coherence Editing: Pulse-field Gradients and Phase Cycling

Instruction for Operating the Bruker Avance III 800 MHz NMR Spectrometers in UTMB

The Agilent OneNMR Probe

(N)MR Imaging. Lab Course Script. FMP PhD Autumn School. Location: C81, MRI Lab B0.03 (basement) Instructor: Leif Schröder. Date: November 3rd, 2010

Exercise at the Spectrometer

Fourier Transform. louder softer. louder. softer. amplitude. time. amplitude. time. frequency. frequency. P. J. Grandinetti

NMR FACILITY NEWSLETTER

ENGR 210 Lab 12: Sampling and Aliasing

List of Commands and Parameters

MT-540. D-Ribavirin, [ 3 H]- Lot A DG

KJM Version 1.0. Topspin 3.5 Windows 7 Topspin 1.3 Windows XP

The operation manual of spotlight 300 IR microscope

ENSC327 Communication Systems Fall 2011 Assignment #1 Due Wednesday, Sept. 28, 4:00 pm

Principios Básicos de RMN en sólidos destinado a usuarios. Gustavo Monti. Fa.M.A.F. Universidad Nacional de Córdoba Argentina

MT Gemcitabine, [5-3 H(N)]- Lot A NK

EEL 4350 Principles of Communication Project 2 Due Tuesday, February 10 at the Beginning of Class

Laboratory Experiment #1 Introduction to Spectral Analysis

Acceptance Solid State NMR Test Procedure. for Avance NMR Systems

Development of an Enantioselective Route towards the. Lycopodium Alkaloids: Total Synthesis of Lycopodine.

γ-trifluoromethyl proline: Evaluation as a structural substitute of proline for solid state 19 F-NMR peptide studies

Lab 8 6.S02 Spring 2013 MRI Projection Imaging

Arrayed Acquisition in VNMR and on the Gemini 1

Seized Drugs Operational Guidelines for the Thermo FTIR Comparative and Analytical Division

COMMUNICATIONS Volume-Selective Multipulse Spin-Echo Spectroscopy

Nutation Spectra of Nuclear Quadrupole Resonance in Off-Resonance Conditions

TUTORIAL PROGRAM FID (Windows 95 Version)

Reference Manual SPECTRUM. Signal Processing for Experimental Chemistry Teaching and Research / University of Maryland

Arenium Acid-Catalyzed Deuteration of Aromatic Hydrocarbons

The Multidimensional Filter Diagonalization Method

Setting up a Multi sine impedance measurement

Instruction manual for T3DS software. Tool for THz Time-Domain Spectroscopy. Release 4.0

Avance GRASP. Installation/User Manual BRUKER. Version

Workshop on Rapid Scan EPR. University of Denver EPR Center and Bruker BioSpin July 28, 2013

B12. SIMPSON Exercises

Supplementary Information

Recording EPR Spectra using ER 4102ST Resonator

2015 Spin echoes and projection imaging

Qualion NMR Process\Lab NMR (Nuclei Magnetic Resonance) Analyzer Model MASH, Style D

Quadrature Amplitude Modulation (QAM) Experiments Using the National Instruments PXI-based Vector Signal Analyzer *

NOVA technical note #8 1. Case study: how to use cutoff conditions in a FRA frequency scan?

Nuclear Magnetic Resonance Spectrometer (600MHz)

Efficacy of Wavelet Transform Techniques for. Denoising Polarized Target NMR Signals

Introduction to Simulink Assignment Companion Document

In a typical biological sample the concentration of the solute is 1 mm or less. In many situations,

Experiment 2: Electronic Enhancement of S/N and Boxcar Filtering

Renishaw InVia Raman microscope

Lab 1B LabVIEW Filter Signal

SpinCore RadioProcessor LabVIEW Extensions

LLS - Introduction to Equipment

MEASUREMENT AND MINIMIZATION OF FIELD INHOMOGENEITIES IN HIGH RESOLUTION NMR

1 Introduction. 2 The basic principles of NMR

Advanced Lab LAB 6: Signal Acquisition & Spectrum Analysis Using VirtualBench DSA Equipment: Objectives:

Gentec-EO USA. T-RAD-USB Users Manual. T-Rad-USB Operating Instructions /15/2010 Page 1 of 24

Temps can range -130 to +120 C. See instructions below (part I). Such data can also be acquired on Athena and the AVANCE-360.

ET 304A Laboratory Tutorial-Circuitmaker For Transient and Frequency Analysis

Figure AC circuit to be analyzed.

Reading: Johnson Ch , Ch.5.5 (today); Liljencrants & Lindblom; Stevens (Tues) reminder: no class on Thursday.

ECG Analysis using the Offline Averaging Mode

Transcription:

Chapter HMBC 17 Introduction 17.1 Goto Heteronuclear Multiple Bond Correlation spectroscopy is a modified version of HMQC suitable for determining long-range 1 H- 13 C connectivity. This is useful in determining the structure and 1 H and 13 C assignments of molecules. Since it is a long-range chemical shift correlation experiment, HMBC provides basically the same information as COLOC; however, since it is also an inverse experiment, HMBC has a higher sensitivity than COLOC. The HMBC pulse sequence may be described simply as follows: The first 13 C 90 pulse, which occurs 1/(2 1 J XH ) after the first 1 H 90 pulse, serves as a low-pass J- filter to suppress one-bond correlations in the 2D spectrum. It does this by creating heteronuclear multiple quantum coherence for 1 H s directly coupled to a 13 C nucleus. This unwanted coherence is removed from the 2D spectrum by phase cycling the first 13 C 90 pulse with respect to the receiver. After the interval 2 (which is about 60 msec), the second 13 C 90 pulse creates the desired heteronuclear multiple quantum coherence for 1 H s J-coupled to a 13 C nucleus 2 or 3 bonds away. This is followed by the evolution time t 1. A 1 H 180 pulse placed halfway through t 1 removes the effect of 1 H chemical shift from the t 1 modulation frequency. The final 13 C 90 pulse occurs directly after the evolution period, and is followed immediately by the detection period t 2. After the final 13 C 90 pulse, the 1 H signals originating from 1 H- 13 C multiple quantum coherence are modulated by 13 C chemical shifts and homonuclear 1 H J-couplings. Phase cycling of the second 13 C 90 pulse removes signal from 1 H s that do not have a long-range coupling to 13 C. The signal detected during t 2 is phase modulated by the homonuclear 1 H J- couplings. The 2D spectrum is generated by a Fourier transform with respect to t 1 and t 2. Because of phase modulation, the final spectrum has peaks which are a combination of absorption and dispersion lineshapes. It is not possible to phase correct the spectrum so that the peaks are purely absorptive, and so the spectrum must be presented in magnitude mode. If more than one long-range 1 H- 13 C connectivity is detected for one particular proton, the relative intensities of the corresponding resonances are directly related to the magnitude of the coupling constant. Reference: A. Bax and M. F. Summers, J. Am. Chem. Soc., 108, 2093 (1986). Sample The sample used to demonstrate HMBC in this chapter is 50mM Gramicidin in DMSO-d6. This is the same sample that was used to demonstrate COSY, NOESY, ROESY, and TOCSY, and HMQC. AVANCE User s Guide Bruker 185

HMBC Pulse Sequence Diagram 17.2 The HMBC pulse sequence is shown in Figure 49. Notice that the pulses p1 and p3 must be set to the appropriate 90 times found in Chapter 5 Pulse Calibration. The 180 pulse length p2 is determined by the pulse program itself. Figure 49: HMBC Pulse Sequence π 2 π 1 H d1 p1 d2 d6 d0 p2 d0 acq t 2 π π 2 2 1 1 t 1 13 C t rd n JXH 2 2J XH t 1 2 π 2 p3 p3 p3 Acquisition and Processing 17.3 Make sure the following preliminary steps have been completed: Insert the sample in the magnet. Lock the spectrometer. Readjust the Z and Z 2 shims until the lock level is optimized. Tune and match the probehead for 1 H observation 13 C decoupling. It is generally recommended that HMBC, like all 2D experiments, be run without sample spinning. 1 H reference spectrum Since HMBC is a 1 H-observe experiment, the first step is to obtain a reference 1 H spectrum of the sample. This reference spectrum will be used to determine the correct o1 for 1 H, the correct sw for the F2 dimension, and can also be used as the F2 projection of the HMBC spectrum. A 1 H reference spectrum of this sample was already created for the magnitude COSY experiment. This spectrum is found in the data set proton/5/1. 13 C reference spectrum It can be assumed that the sample used for an inverse experiment such as HMBC has too small a 13 C signal to make it practical to obtain a 13 C reference spectrum. Thus, the user will need to make an educated guess as to the appropriate values of o2 and 186 Bruker AVANCE User s Guide

Acquisition and Processing sw for the F1 dimension. Actually, it is easier to use o2p (in ppm) rather than o2 (in Hz). This is because the UXNMR lock routine was used to lock the magnetic field, and so 0ppm (for a given nucleus) is at the same absolute frequency regardless of the lock solvent. Note that because HMBC is a multiple bond correlation experiment, we can expect to detect signals from 1 H s coupled to quaternary 13 C s, in addition to primary, secondary and tertiary 13 C s. Thus, the 13 C spectral width should be larger than that used for HMQC. An appropriate spectral width would cover the range from 10ppm to 250 ppm. This corresponds to an o2p value of 120 ppm and an sw value of 260 ppm. Create a new file directory for the 2D data set Enter re proton 5 1 to return to the optimized 1 H spectrum. From this data set, enter edc and change the following parameters: NAME hmbc EXPNO 1 PROCNO 1. Click SAVE to create the data set hmbc/1/1. By creating the HMBC data set from data set of the 1 H reference spectrum, most of the F2 parameters for HMBC are already set. Enter edsp and set NUC2 to 13C and OFSH1 to o1 of the 1 H reference spectrum proton/5/1. The parameter OFSX1 should have the value of o2 corresponding to o2p = 120ppm, but the best way to set this is simply to set o2p correctly in the main UXNMR window. Change to 2D parameter mode Enter eda and set PARMODE = 2D. Click on SAVE and ok the message Delete meta.ext files?. The window now switches to a 2D display and the message NEW 2D DATA SET appears. Set up the acquisition parameters Enter eda and set the acquisition parameters as shown in Table 51. Use the values determined in Chapter 5 Pulse Calibration for the parameters pl1 and p1 ( 1 H observe high power level and 90 pulse time), and pl2 and p3 ( 13 C decouple high power level and 90 pulse time). Note that the pulse program inv4lplrnd calls an include file in which cnst2 is used to calculate d2 (d2 = 1/(2*cnst2)). Thus, it is only necessary for the user to set the value of cnst2. Similarly, the 180 pulse length p2 is calculated from the corresponding 90 pulse length p1, so the user need only set the value of p1. On the other hand, d6 is not defined in the include file, and so must be set explicitly in eda. The F2 parameters o1 and sw (not shown in the table) should be identical to the values used in the optimized 1 H reference spectrum (proton/5/1). Make sure to set o2p to 120ppm as discussed above. The F1 parameter sw should also be set to 260 ppm as discussed above. Finally, notice that in0 and sw(f1) are not independent. A convenient way to set in0 is to set the F1 parameters nuc1 by clicking NUCLEI for F1 parameters, nd0, and sw correctly. This automatically sets in0 to the correct value. AVANCE User s Guide Bruker 187

HMBC Table 51. HMBC Acquisition Parameters F2 Parameters Parameter Value Comments PULPROG inv4lplrnd see Figure 49 for pulse sequence diagram. TD 4k NS 64 the number of scans should be 16*n in order for the phase cycling to work properly. DS 32 number of dummy scans. PL1 PL2 P1 P2 P3 high power level on f1 channel (see An Important Note on Power Levels on page 7). high power level on f2 channel (see An Important Note on Power Levels on page 7). 90 1 H high power pulse on f1 channel. 180 1 H high power pulse on f1 channel; calculated internally. 90 13 C high power pulse on f2 channel. D0 3µsec incremented delay (t 1 /2); predefined. D1 1.5sec relaxation delay; should be about 1.25*T 1 ( 1 H). D2 3.45msec delay for creation of anti-phase magnetization (1/(2J XH )); calculated internally. D6 ~50msec delay for evolution of long range couplings (1/( n J XH )). CNST2 145Hz one-bond heteronuclear J-coupling (J XH ). F1 Parameters Parameter Value Comments TD 256 number of experiments. ND0 2 there are two d0 periods per cycle and MC2 = QF. IN0 1/(2*SW X ) = DW X SW NUC1 t 1 increment. sw of the 13 C spectrum (here typically 260ppm). select 13 C frequency for F1 Acquire the 2D data set Enter zg to start the HMBC experiment. With the acquisition parameters shown above, the approximate experiment time is 13.5 hours. 188 Bruker AVANCE User s Guide

Acquisition and Processing Set up the processing parameters Enter edp and set the processing parameters as shown in Table 52. Table 52. HMBC Processing Parameters F2 Parameters Parameter Value Comments SI 2k SF spectrum reference frequency ( 1 H). WDW QSINE multiply data by phase-shifted sine-squared function. SSB 0 (4) choose pure sine wave (or optimize the phase shift of the sine-squared function). PH_mod no this is a magnitude spectrum. PKNL TRUE necessary when using the digital filter. BC_mod quad F1 Parameters Parameter Value Comments SI 256 SF spectrum reference frequency ( 13 C). WDW SINE multiply data by phase-shifted sine function. SSB 2 choose pure cosine wave. PH_mod mc this is a magnitude spectrum. BC_mod MC2 QF determines type of FT in F1; QF results in a forward quadrature complex FT. Process the 2D data set It is especially useful to do an automatic baseline correction in the F1 dimension of this 2D spectrum, in part because HMBC spectra usually have quite a bit of t 1 noise and also because they are magnitude mode. Enter xfb to multiply the time domain data by the window functions and also perform the 2D Fourier transform. Adjust the contour levels The threshold level can be adjusted by placing the cursor on the holding down the left mouse button, and moving the mouse up and down. button, Since this is a magnitude spectrum, click on +/- with the left mouse button until only the positive peaks are displayed. AVANCE User s Guide Bruker 189

HMBC The optimum display (both the threshold and which peaks are displayed) may be saved by clicking on DefPlot. Phase correct the spectrum Since this is a magnitude spectrum, no phase adjustment can be made. Plot the spectrum Read in the plot parameter file standard2d, e.g., enter rpar standard2d plot. This sets most of the plotting parameters to values which are appropriate for this 2D spectrum, assuming that the paper size to be used here is the same as the default paper size defined when the spectrometer was configured. More information about plotting parameters and the file standard2d can be found in Appendix C 1D and 2D Plotting Parameters. To set the region (full or expanded), threshold, and peak type (positive and/or negative), to be used in plotting the spectrum, first make sure the spectrum appears as desired on the screen, and then click DefPlot and answer the following questions. Change levels? y Please enter number of positive levels? 6 Display contours? n. Enter edg to edit the plotting parameters. Click the ed next to the parameter EDAXIS to enter the axis parameters submenu. Change the value of the parameter X2TICD from 0.1 to 2.5. Click SAVE to save this change and return to the edg menu. Since there is no 13 C reference spectrum of this sample, the user may choose not to plot an F1 projection for the HMBC spectrum. To do this, simply click the YES adjacent to PROJ1 in the edg menu to toggle it to NO. Click the ed next to the parameter EDPROJ2 to enter the F2 projection parameters submenu. Edit the parameters from PF2DU to PF2PROC as follows: PF2DU u PF2USER (name of user for file proton/5/1) PF2NAME proton PF2EXP 5 PF2PROC 1. Click SAVE to save these changes and return to the edg menu. Click SAVE to save all the above changes and exit the edg menu. Next create a title for the spectrum. Enter setti to use the editor to open the title file. Write a title and save the file. To plot the spectrum, simply enter plot (provided the correct plotter is selected in edo). An HMBC spectrum of 50mM Gramicidin in DMSO-d6 is shown in Figure 50. 190 Bruker AVANCE User s Guide

Acquisition and Processing Figure 50: HMBC Spectrum of 50 mm Gramicidin in DMSO-d6 ppm 20 40 60 80 100 120 140 160 180 8 6 4 2 ppm AVANCE User s Guide Bruker 191

HMBC 192 Bruker AVANCE User s Guide