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In this study, we used two compounds that have a primary sulfonamide group in their structures ( Figure 2) and exhibit sub-millimolar binding affinities for CA I and CA II.
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(48) A full set of spectra for one sample throughout the pressure range was recorded in approximately 20 h with CA I and 30 h with CA II protein samples.
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All NMR experiments were processed with TOPSPIN software (Bruker), and the spectra were analyzed with CcpNmr Analysis V2 software. Water resonance was used as the reference because the most commonly used referencing compound sodium trimethylsilylpropanesulfonate (DSS) might inhibit CA I and CA II. (47) 1H chemical shifts were directly referenced to the water resonance (4.7 ppm), while 15N chemical shifts were referenced indirectly to the 15N/ 1H absolute frequency ratios. Water suppression was achieved using the WATERGATE method. 2D 1H– 15N HSQC spectra were recorded at 25 ☌ and eight different pressures ranging from 5 to 210 MPa on a Bruker AVANCE III 600 MHz equipped with a 5 mM Z-gradient TXI probe head. Hydrostatic pressure was applied to the sample directly within the magnet through an inox line filled with low-density paraffin oil (Sigma) using an Xtreme Syringe Pump from Daedalus Innovations. The protein solution (0.33 mL) was added into a ceramic tube with an outer diameter of 5 mM and an inner diameter of 3 mM from Daedalus Innovations (Aston, PA). High-pressure NMR spectroscopy was used to record 2D 1H– 15N HSQC spectra of CA I and CA II at various pressures. We think that the best way to obtain a complementary view of the protein–ligand binding volume is to use several techniques by exploiting their strengths and overcoming possible weaknesses. (38,39) All mentioned techniques reveal different aspects of protein–ligand interactions and have not only advantages but limitations also. (37) The protein–ligand dissociation constant, K d, can be accurately determined only if the protein concentration is in the range of K d, and thus the micromolar concentration of a protein in the NMR experiment limits the range of possible ligand affinities to weak and moderate. Advantages of NMR spectroscopy come at a price: this assay requires relatively high concentrations of 15N-labeled proteins. Such features are unavailable in density- or fluorescence-based techniques, which provide ensemble-averaged properties, and many details remain hidden. This allows identification of the binding-affected amino acid residues and analyze changes at the ligand binding site. (16,29,35,36) The NMR spectroscopy is particularly informative in volumetric measurements because it can monitor changes in the local amino acid rearrangement.
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Driver Downloader License Key (s): DF12-2RM2-JDPE-NJM6 DF12-2RM2-JDPE-9988 Product License Key (s): Note: Pay careful attention when entering in your license key.Various experimental approaches may be used to measure the protein–ligand binding volume including the density and ultrasound velocity techniques, (23,33) small-angle X-ray and elastic incoherent neutron scattering, (34) fluorescence spectroscopy at elevated pressures, (24,30,31) and high-pressure NMR. License keys are product-specific and will only activate the product with which they are associat ed.
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