NMR Pulse Program Library Website of the Schmidt-Rohr Group

Dept. of Chemistry, Iowa State University, Ames, IA 50011

(Click here for Dr. Mei Hong’s NMR web site)

 

This website provides solid-state NMR pulse programs, most of which were introduced or improved by our group.  It is our goal to make these NMR methods (which were developed with support by tax-payers’ money) more widely available. 

 

Users of Bruker DSX/DRX/Avance spectrometers should be able to run the programs with minor modifications, and may find the parameter files  (click after the “Requires” category where possible) useful.  For users of other platforms, the pulse timings, phase sequences, and comments given should still be useful.

 

Compatibility

With small modifications, the programs should work with Bruker XWINNMR 2.6 to 3.5.  The most likely required change involves the detection commands and the frequency switches. 

- In experiments with regular detection, you may need to copy the detection command from you CP/MAS program to replace the  “go=2     ph31” command

 

- In multiple-pulse experiments with detection between pulses, please copy the detection commands from your MREV-8 or BR-24 programs to replace the ones used in our programs.

 

- For experiments with refocused or multiple-echo detection, we show the more traditional XWINNMR 2.6 as well as the more unusual XWINNMR 3.5 versions.

 

- Frequency switches are shown mostly with the syntax “fq=cnst4: f2”, which works well in XWINNMR 3.5 and is convenient.  In XWINNMR 2.6 and 3.1, we always used pointers “fq4: f2” to frequency lists found in the “f1” subdirectory and accessed through “ased”.

 

Order and Complexity

Within each category, the programs are listed roughly chronologically by publication date. A new program will usually be added at the end of the appropriate category.

 

In the “Requires” line, the simplest experiments are marked by a single !, the most difficult by !!!!!!.

 

WARNING and Disclaimers

The pulse programs provided here are intended only as guides.  We cannot guarantee that they will work on your spectrometer.  Incorrect parameter values, incompatible or malfunctioning pulse programmers, etc., could result in long pulses that may destroy your sample, probehead, preamplifier, and/or transmitter (high-power amp).  You need to check the programs yourself, e.g. using a dummy load and oscilloscope, and adjust all parameters carefully for your system before use. We cannot be held responsible for any loss or damage caused by the use of the pulse programs and/or information provided here.

 

Some comments in the pulse programs may refer to older program versions and may not be accurate.  Some phase lists may not be required in the current program version.

 

For background on the techniques listed, please refer first to the references provided.  We will try to address specific questions, and certainly appreciate warnings, comments, and suggestions.  However, for general questions of how to make pulse programs work on your spectrometer, please contact an application scientist of your spectrometer manufacturer.

 

0)  QUANTITATIVE NMR

This material is based upon work supported by the National Science Foundation under grants No. 0138117 and EEC-0813570.

 

0.1) Program:

MultiCP (with Hahn echo at 2 tr)

Description:

Essentially quantitative cross-polarization 13C spectra, without baseline distortion

Requires:

!!; usually high spinning frequency (e.g. 14 kHz)

Reference(s):

Johnson & Schmidt-Rohr, J. Magn. Reson. 239, 44-49 (2014).

 

 

1.1) Program:

DP/MAS with Hahn echo at 2 tr

Description:

Quantitative 13C spectra (after long recycle delay), without baseline distortion

Requires:

!; high spinning frequency (e.g. 14 kHz)

Reference(s):

Mao et al., Soil Sci. Soc. of Am. J. 64, 873-884  (2000), Mao & Klaus Schmidt-Rohr, Environ. Sci. Technol. 38, 2680-2684 (2004).

 

1)    SPECTRAL EDITING etc.

This material is based upon work supported by the National Science Foundation under grant No. 0138117. Any opinions, findings, and conclusions or recommendations expressed in this material are those of author(s) and do not necessary reflect the views of the National Science Foundation.

 

 

 

1.2) Program:

DP/MAS with dipolar dephasing at high spinning speed

Description:

Quantitative 13C spectra of unprotonated C

Requires:

!; high spinning frequency (e.g. 14 kHz)

Reference(s):

Mao & Schmidt-Rohr, Environ. Sci. Technol. 38, 2680-2684 (2004).

 

 

1.3) Program:

CP/T1/TOSS

Description:

Use to determine recycle delay for DP/MAS

Requires:

!; few scans per hour, best with large rotors and therefore moderate spinning frequency (6.5 kHz)

Reference(s):

Mao et al., Soil Sci. Soc. of Am. J. 64, 873-884  (2000), Mao & Schmidt-Rohr, Environ. Sci. Technol. 38, 2680-2684 (2004).

 

 

1.4) Program:

Dipolar DEPT for CH-only spectra

Description:

Selects CH (methyne) signals

Requires:

!!!! first set-up; !! run routinely (ca. 15% effic.).  Higher power during ca. 2.16 tr = 540 us; 4 or 5.8 kHz MAS

Reference(s):

Schmidt-Rohr & Mao, J. Am. Chem. Soc. 124, 13938-13948 (2002).

Applied in:

Mao et al., Environ. Sci. Technol. 37, 1751-1757 (2003).

 

 

1.5) Program:

Recoupled long-range dipolar dephasing and its Reference sequence

Description:

13C{1H}REDOR, selects nonprotonated aromatic carbons far from protons (e.g. charcoal)

Requires:

!!; DP/TOSS at ca. 7 kHz MAS

Reference(s):

Mao & Schmidt-Rohr, J. Magn. Reson. 162, 217-227 (2003).

 

 

1.6) Program:

SPIDER (Saturation-Pulse-Induced Dipolar Exchange with Recoupling)

Description:

Selects C bonded to N

Requires:

!!!!!; 1H-14N-13C triple-resonance equipment,  5 kHz MAS

Reference(s):

Schmidt-Rohr & Mao, Chem. Phys. Lett. 359, 403-411 (2002), Schmidt-Rohr, Mao, Olk, Proc. Nat. Acad. Sci. 101, 6351-6354 (2004).

 

 

1.7) Program:

Reference S00 pulse sequence with minimized effects of longitudinal quadrupolar relaxation

Description:

Minimize the effects of longitudinal quadrupolar relaxation on the sub-millisecond time scale on reference signal S0 in experiments on S-L heteronuclear spin systems with evolution of the S-spin magnetization under the influence of a quadrupolar nucleus, such as REDOR, REAPDOR, RIDER, or SPIDER.

Requires:

!!!; choose odd numbers for l0,  5 kHz MAS.

Reference(s):

Hu & Schmidt-Rohr J.Magn. Reson. 197, 193-207 (2009).

 

 

1.8) Program:

RIDER (Relaxation-Induced Dipolar Exchange with Recoupling)

Description:

Selects C bonded to N (and slowly rotating segments)

Requires:

!!; Same pulse sequence as CODEX; in contrast to SPIDER, only 1H-13C double-res. equipment is needed; but slow dynamics will produce artifacts.

Reference(s):

Saalwächter & Schmidt-Rohr, J. Magn. Reson. 145, 161-172 (2000).

 

 

1.9) Program:

CSA filter:  3-pulse version,  5-pulse version , 5-pulse version 2

Description:

Selects alkyl (i.e. sp3-hybridized) C, e.g. O-C-O (which overlap with aromatic C) by three- or five-pulse CSA dephasing

Requires:

!!; 5-7 kHz MAS; short CP for O-CH-O selection; long CP & gated decoupling for O-Cq-O selection

Reference(s):

Mao & Schmidt-Rohr, Solid State NMR 26, 36-45 (2004); compare SUPER sequence (5.3) for measurement of all three CSA principal values

 

 

1.10) Program:

CH2 spectral editing by selection of three-spin coherence

Description:

Selects CH2 (methylene) signals

Requires:

!!!! first set-up; !!! run routinely (ca. 6% effic.).  Higher power during tr = 140 us; 5.8 kHz MAS

Reference(s):

Mao & Schmidt-Rohr, J. Magn. Reson. 176, 1-6 (2005)

 

1’) SPECTRAL EDITING OF 2D SPECTRA OF 13C-ENRICHED PROTEINS/ MATERIALS

The following work has been authored at the Ames Laboratory and Iowa State University of Science and Technology with support from the U.S. Department of Energy, Office of Basic Energy Sciences, Division of Materials Sciences and Engineering under Award AL-90-360-001. The views and opinions of authors expressed herein do not necessarily state or reflect those of the United States Government or Iowa State University, and shall not be used for advertising or product endorsements purposes.

1'.1) Program:

CN-free 2D CC Spectroscopy (COO selection)

Description:

Selects signals of Glu and Asp by retaining COO magnetization

Requires:

!! Fairly simple combination of REDOR and 2D 13C-13C NMR, good sensitivity, 8 – 12 kHz MAS

Reference(s):

 Schmidt-Rohr et al., J. Biomol. NMR 56, 155-167 (2012)

Applied in:

Fritzsching et al., to be submitted

 

 

1'.2) Program:

CH-selected 2D CC Spectroscopy

Description:

Selects signals of Ile, Val, and Leu by sidechain CH-selection

Requires:

!!!! first set-up, !!! run routinely; moderate sensitivity, 8 – 12 kHz MAS

Reference(s):

 Schmidt-Rohr et al., J. Biomol. NMR 56, 155-167 (2012)

Applied in:

Fritzsching et al., to be submitted

 

 

1'.3) Program:

Dynamics-edited 2D CC Spectroscopy

Description:

Selects signals of mobile CH2 (& CH3) groups by recoupled dipolar dephasing

Requires:

!! 2D CC with preequilibration and gated decoupling, good efficiency

Reference(s):

 Schmidt-Rohr et al., J. Biomol. NMR 56, 155-167 (2012)

 

The following material is based upon work supported by the National Science Foundation under grant No. EEC-0813570. Any opinions, findings, and conclusions or recommendations expressed in this material are those of author(s) and do not necessary reflect the views of the National Science Foundation.

 

1'.4) Program:

2D EXPANSE Spectroscopy

Description:

2D CH-Cnonp correlation without diagonal ridge, for 13C-enriched carbon materials

Requires:

!!!!; 14 kHz MAS (at 9.4T)

Reference(s):

Johnson et al., Solid State NMR 234, 112-124 (2013)

 

 

1'.5) Program:

Dipolar-dephased DQ/SQ 2D Spectroscopy

Description:

2D Cnonp-Cnonp correlation (without diagonal ridge), for 13C-enriched carbon materials

Requires:

!!; 14 kHz MAS (at 9.4T)

Reference(s):

Johnson et al., Solid State NMR 234, 112-124 (2013)

 

2) 2D HETCOR FOR SITE IDENTIFICATION

 

NOTE: The FSLG as programmed in the following HETCOR experiments probably works only in the specified XWINNMR version.  You may need to replace it by your own version of FSLG.

 

2.1) Program:

1H- 13C HETCOR

Description:

1H-13C HETCOR with FSLG decoupling and LGCP transfer

Requires:

!!!; higher power for good 1H resolution; 6 - 12 kHz MAS

Reference(s):

HETCOR has been used and improved by various groups, after the pioneering work of Caravatti et al., Chem. Phys. Lett., 100, 305 (1983). Also compare HETCOR with fast MAS at high field (Spiess et al.)

 

 

2.2) Program:

MELODI (MEdium and LOng Distance) HETCOR

Description:

Suppresses the mostly trivial one-bond 1H-13C peaks in HETCOR

Requires:

!!!!; 

Reference(s):

Yao, Schmidt-Rohr, Hong, J. Magn. Reson. 149, 139-143 (2001).

 

 

2.3) Program:

HETCOR after 1H CSA filter

Description:

Suppresses NH/OH signals in HETCOR spectra (overlap with aromatic H)

Requires:

!!!!!; 

Reference(s):

Schmidt-Rohr & Mao, J. Magn. Reson. 157, 210-217 (2002).

 

Most of the following work has been authored at Iowa State University of Science and Technology under Contract No. W-7405-ENG-82 with U.S. Department of Energy.  The views and opinions of authors expressed herein do not necessarily state or reflect those of the United States Government or Iowa State University, and shall not be used for advertising or product endorsements purposes.

 

3) 1H SPIN DIFFUSION WITH 13C/29Si DETECTION (HETCOR, CHHC)

 

3.1) Program:

1H- 13C HETCOR with 1H spin diffusion

Description:

1H-13C HETCOR with FSLG decoupling and LGCP transfer

Requires:

!!!;  faster spinning (6 - 12 kHz)

Reference(s):

Another version of HETCOR with spin diffusion was used widely by P. Mirau, J. White, et al.

 

 

3.2) Program:

1H-29Si HETCOR with refocused detection and 1H spin diffusion. (XWINNMR 2.6 and XWINNMR 3.5)

Hartmann-Hahn CP transfer and MREV-8 decoupling version, Hartman-Hahn CP transfer and FSLG decoupling version,

LGCP transfer and MREV-8 decoupling version, LGCP transfer and FSLG decoupling version

Description:

Sensitivity-enhanced detection of organic segments near silicate surfaces in composites of organic materials with nanosize silicates

Requires:

!!!;  set 29Si signal on resonance

Reference(s):

Hou et al. Solid State NMR 22, 110-127 (2002), and Macromolecules 36, 2769-2776 (2003).

 

 

3.3) Program:

HETCOR after on-resonance 1H chemical-shift filter

Description:

Suppression of dominant signals in HETCOR to reveal small bands

Requires:

!!!;

Reference(s):

Schmidt-Rohr & Mao, unpublished

 

 

3.4) Program:

CHHC with MAD (Multiple Alternating Depolarization)

Description:

2D 13C-13C NMR with cross peaks due to 1H spin diffusion

Requires:

!!!; long measuring times at long mixing times (2% efficiency)

Reference(s):

Hou, Chen, & Schmidt-Rohr, Macromolecules 37, 1999-2001 (2004).

 

 

4) 1H NMR

 

4.1) Program:

1H background suppression

Description:

Probehead background suppression in 1H one-pulse spectra

Requires:

!;  static or MAS spectra

Reference(s):

Chen & Schmidt-Rohr, Solid State NMR 26, 11-15 (2004)

 

 

4.2) Program:

1H CRAMPS after 1H CSA filter

Description:

Suppression of NH/OH signals in 1H CRAMPS spectra

Requires:

!!!!;  relatively slow MAS

Reference(s):

Schmidt-Rohr & Mao, J. Magn. Reson. 157, 210-217 (2002).

 

 

4.3) Program:

PRIDE (PRoton Inverse-detected Deuteron) NMR by HMQC and pulsed 1H spin-lock

Description:

Sensitivity-enhanced deuteron NMR of partially deuterated systems by 1H detection

Requires:

!!!!;  static 2D experiment

Reference(s):

Schmidt-Rohr et al., J. Am. Chem. Soc. 123, 7168-7169 (2001).

                       

 

5) DYNAMICS

 

5.1) Program:

CODEX (Centerband-Only Detection of Exchange)

Description:

Detection of slow (1-ms to 10-s) exchange dynamics under MAS of any spinning frequency

Requires:

!!!;  rotation-synchronized mixing time (MAS trigger)

Reference(s):

de Azevedo et al., J. Am. Chem. Soc. 121, 8411-8412 (1999) and J. Chem. Phys. 112, 8988-9001  (2000); Reichert, Bonagamba, Schmidt-Rohr, J. Magn. Reson. 151, 129-135 (2001).

 

 

5.2) Program:

PUREX (PURE-EXchange) NMR

Description:

2D exchange experiment with suppression of the diagonal signal (ridge) and its artifacts

Requires:

!!!;

Reference(s):

de Azevedo, Bonagamba, Schmidt-Rohr J. Magn. Reson. 142, 86-96 (2000).  A somewhat more sensitive version was recently introduced by N. Nielsen.

 

 

5.3) Program:

SUPER (Separation of Undistorted Powderpatterns by Effortless Recoupling)

Description:

Separation of regular chemical-shift anisotropy powder patterns of dilute spins (13C, 29Si) with 0.155 scaling factor

Requires:

!!!; 2.5 - 4 kHz MAS, 13C w1 = 12.12 wr, 1H w1 = 30 wr.

Reference(s):

Liu, Mao, & Schmidt-Rohr, J. Magn. Reson. 155, 15-28 (2002).

 

 

5.4) Program:

WISE (2D 1H WIdeline SEparation by 13C chemical shifts) with LGCP

Description:

Detect fast rotational dynamics by 1H line narrowing with 13C site resolution

Requires:

!!;

Reference(s):

Schmidt-Rohr, Clauss, Spiess, Macromolecules 25, 3273-3277 (1992).  This program also includes 13C decoupling during t1 introduced by Tekely et al., 

Recent application of this specific pulse sequence: Schmidt-Rohr & Mao, J. Am. Chem. Soc. 124, 13938-13948 (2002).

                       

6) FLUOROPOLYMERS

 

6.1) Program:

13C CP NMR with fast MAS (>25 kHz) and pulsed 19F decoupling

Description:

High-resolution 13C spectra of fluoropolymers

Requires:

!!!!!; fast spinning (>14 kHz); demanding set-up due to narrow CP condition and small signal of small sample.

Reference(s):

Liu & Schmidt-Rohr, Macromolecules 34, 8416-8418 (2001).

 

 

6.2) Program:

19F-13C HETCOR

Description:

One-bond correlations of 19F and 13C peak positions in fluoropolymers

Requires:

!!!!;  little difficulty after 6.1)

Reference(s):

Chen & Schmidt-Rohr, Macromolecules 37, 1999-2001 (2004)

 

 

6.3) Program:

2D 19F exchange NMR with fast MAS (>25 kHz)

Description:

Determine proximity of various 19F sites

Requires:

!!;

Reference(s):

Chen & Schmidt-Rohr, Macromolecules 37, 1999-2001 (2004)

 

7) DETERMINATION OF PARTICLE THICKNESS

 

7.1) Program:

HARDSHIP (HeteronucleAr Recoupling with Dephasing by Strong Homonuclear Interactions of Protons), reference sequence

Description:

Determine the thickness of phosphate, silicate, carbonate, and other nanoparticles in organic-inorganic nanocomposites

Requires:

!!!;  relatively fast MAS (ca. 13 kHz), usually l5=3, l6=1

Reference(s):

Schmidt-Rohr, Rawal, & Fang, J. Chem. Phys126 (5),  2007

 

8) 125Te NMR (ALSO FOR OTHER HIGH-Z ISOTOPES)

        

8.1) Program:

Fast Magic Angle Turning: acquisition of the regular dataset, acquisition of the time-reversed dataset, acquisition of t1=0 row, data acquisition and processing procedure, matlab code for offline data processing.

Description:

Separates CSA and isotropic chemical shift, to obtain sideband-free spectra, e.g. for high-Z spin-1/2 nuclei in a non-cubic environment; a broadband method, works for spectra that are up to 1.8 gB1 wide.

Requires:

!!!; pulse power level should be at least 0.55 of the total spectral width of interest. 70o and 140o can be used instead of 90o and 180o pulses, respectively, for the widest excitation profile.

Reference(s):

Hu & Schmidt-Rohr, J. Am. Chem. Soc., 131, 8390-8391 (2009), Solid State Nucl. Magn. Reson. (Technical Aspects of Fast Magic-Angle Turning NMR for Dilute Spin-1/2 Nuclei with Broad Spectra), in press.

 

Prof. Klaus Schmidt-Rohr

Tel : 515-294-6105
Email :
srohr@iastate.edu

http://www.chem.iastate.edu/faculty/Klaus_Schmidt-Rohr/
Comments/ Suggestions/ Queries: kfritzsc@iastate.edu