For NMR experiments, 0.1 mM purified wild-type and mutant HopZ1a proteins, in the absence or presence of 1 mM IP6, were dissolved in 500 μl of buffer containing 20 mM sodium phosphate (pH 7.5), 150 mM NaCl and 10% D2O. 1D proton NMR spectra (256 scans each) were collected for HopZ1a proteins on a Bruker Advance 600 MHz NMR spectrometer (Bruker Inc., Billerica, MA, USA) equipped with a TXI probe at 25°C. The NMR spectra were then processed and analyzed using the TOPSIN software (Bruker).
Topsin software
Manufactured by Bruker
TOPSPIN is a software package developed by Bruker for the acquisition, processing, and analysis of nuclear magnetic resonance (NMR) data. It provides a user-friendly interface for controlling NMR spectrometers and performing various NMR experiments. TOPSPIN enables the collection, processing, and visualization of NMR data, allowing users to extract valuable information from their samples.
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Lab products found in correlation
2 protocols using topsin software
1
NMR Analysis of HopZ1a Protein
2
TssL Transmembrane Segment Structural Characterization
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A synthetic peptide, corresponding to the TssL transmembrane segment (residues Met183-Ala207) with two additional lysine residues at the N-and C-terminus of the peptide (sequence: KKMYWLSWGAGIVTLAGLWCVLSSVLAKK) was synthesized by Schafer-N (Danemark). Two samples were prepared, one in H 2 O and one in D 2 O for proton/deuterium exchange experiments. For each sample 2 mg of peptide were solubilized in 500 µL of D25-Sodium Dodecyl Sulfate 1%, in 10 mM KH 2 PO4, 1 mM D10-Dithiothreitol, pH 4.5. TOCSY and NOESY experiments were recorded at 300 K using a Bruker Avance III 600 spectrometer equipped with a TCI cryoprobe. Mixing time for the NOESY experiments was 300 ms. The NMR spectra were processed with Topsin software (Bruker) and proton assignment was obtained using the CARA software [75] .
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