Nmrpipe nmrdraw

Manufactured by Bruker

Sourced in Germany

NMRPipe/NMRDraw is a software suite developed by Bruker for the processing and analysis of nuclear magnetic resonance (NMR) spectroscopy data. It provides tools for import, processing, visualization, and analysis of NMR spectra.

Automatically generated - may contain errors

Lab products found in correlation

Xwin nmr software, by Bruker (1 mentions) Drx 500 spectrometer, by Bruker (1 mentions) Avance 3 hd spectrometer, by Bruker (1 mentions) Avance spectrometer, by Bruker (1 mentions) Topspin 4, by Bruker (1 mentions) Topspin 3.5pl7, by Bruker (1 mentions) 800 mhz spectrometer, by Bruker (1 mentions)

Spelling variants of this product

NMRPipe (39 citations)

3 protocols using nmrpipe nmrdraw

NMR Spectroscopy of Organic Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols

Nuclear magnetic resonance (NMR) spectra were acquired at 283 K on a Bruker DRX-500 spectrometer equipped with a triple resonance probe with an x, y, and z-shielded pulsed-field gradient coil. Two-dimensional (2D) NMR spectra were recorded in a phase-sensitive mode using time proportional phase increment for quadrature detection in the t₁ domain. Total correlation spectroscopy (TOCSY)22 using a dipsi-2 spinlock pulse sequence with a mixing time of 70 ms and nuclear overhauser enhancement spectroscopy (NOESY)23 with mixing times of 250–600 ms were performed. All NMR spectra were acquired with 2048 complex data points in t2 and 256 increments in the t1 dimension, with 64 scans per each increment. All NMR data were processed using nmrPipe/nmrDraw or XWIN-NMR software (Bruker Instruments, Karlsruhe, Germany) and analyzed using the Sparky 3.95 program.

Park B.M., Kim E.J., Nam H.J., Zhang D., Bae C.H., Kang M., Kim H., Lee W., Bogen B, & Lim S.K. (2017). Cyclized Oligopeptide Targeting LRP5/6-DKK1 Interaction Reduces the Growth of Tumor Burden in a Multiple Myeloma Mouse Model. Yonsei Medical Journal, 58(3), 505-513.

+ Open protocol

+ Expand

Multinuclear NMR Spectroscopy of Biomolecules

Check if the same lab product or an alternative is used in the 5 most similar protocols

One-dimensional ³¹P NMR experiments were performed on a Bruker Avance spectrometer with a homebuilt ¹H/³¹P double-resonance probe [53 (link)], at a ¹H resonance frequency of 700 MHz. The ³¹P NMR spectra were obtained at 35°C by direct single pulse excitation with a radio frequency (RF) field strength of 50 kHz, 10 ms acquisition time, 2 s recycle delay, and co-addition of 64 transients. Continuous wave ¹H decoupling, with RF field strength of 25 kHz, was applied during data acquisition. ³¹P chemical shifts were externally referenced to phosphoric acid solution at 0 ppm.
Two-dimensional ¹H/¹⁵N separated local field (SLF) NMR experiments were performed using the SAMPI4 pulse sequence [54 (link)], on a Bruker Avance III HD spectrometer with a home-built low-E ¹H/¹⁵N double-resonance probe [55 (link)], at a ¹H resonance frequency of 900 MHz. Signal averaging required 64–512 transients for each of 64–128 t1 increment. The NMR data were processed using Bruker Topspin 4.0.7 and NMRPipe/NMRDraw [56 (link)]. The data were zero-filled to form a final 2048 × 2048 matrix. ¹⁵N chemical shifts were externally referenced to ¹⁵N labeled ammonium sulfate powder at 26.8 ppm.

Park S.H., Wu J., Yao Y., Singh C., Tian Y., Marassi F.M, & Opella S.J. (2020). Membrane proteins in magnetically aligned phospholipid polymer discs for solid-state NMR spectroscopy. Biochimica et biophysica acta. Biomembranes, 1862(9), 183333.

+ Open protocol

+ Expand

NMR Spectroscopy Protocols for Protein Structure

Check if the same lab product or an alternative is used in the 5 most similar protocols

All NMR experiments were recorded at 10 °C for R2* and 4 °C for PRR2* on a Bruker 800 MHz spectrometer equipped with a cryogenic probe. All spectra were processed with topspin 3.5pl7 (Bruker) and NMRPipe/NMRDraw. The assignment of tau PRR2* and R2* was based on a series of 3D spectra using a uniformly ¹⁵N,¹³C-labeled sample including HNCACB, CBCA(CO)NH, HNCO, and HN(CA)CO. ¹H-¹⁵N HSQC experiments were recorded with 8 scans, a recycle delay of 1.0 s, 3072 (t₂) × 200 (t₁) complex data points, and a spectral width of 16 ppm in the ¹H dimension and 22 ppm in the ¹⁵N dimension. HNCACB and CBCACONH were recorded with 8 scans, 3072 (t₃) × 75 (t₁) × 256 (t₂) data points, and a spectral width of 10 ppm in the ¹H dimension, 22 ppm in the ¹⁵N dimension, and 60 ppm in the ¹³C dimension. HNCO and HN(CA)CO were recorded with 8 scans and 32 scans, respectively; 3072 (t₃) × 74 (t₁) × 128 (t₂) data points; and a spectral width of 10 ppm in the ¹H dimension, 22 ppm in the ¹⁵N dimension, and 13 ppm in the ¹³C. Linear prediction and zero-filing were used to obtain complex data matrixes before Fourier transformation to improve resolution.

Murray A., Yan L., Gibson J.M., Liu J., Eliezer D., Lippens G., Zhang F., Linhardt R.J., Zhao J, & Wang C. (2022). Proline-Rich Region II (PRR2) Plays an Important Role in Tau–Glycan Interaction: An NMR Study. Biomolecules, 12(11), 1573.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!