Inova 600 mhz spectrometer

Manufactured by Bruker

The Inova 600 MHz spectrometer is a nuclear magnetic resonance (NMR) instrument designed for high-resolution spectroscopy. It operates at a magnetic field strength of 600 MHz, providing high-quality data for a wide range of applications in chemistry, biochemistry, and materials science.

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Lab products found in correlation

Jnm eca 600 mhz spectrometer, by JEOL (1 mentions) Delta nmr software, by JEOL (1 mentions) 750 mhz spectrometer, by Bruker (1 mentions) Avance 3 850 mhz spectrometer, by Bruker (1 mentions)

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Inova 600 MHz 600 MHz spectrometer INOVA 600 Inova spectrometer Bruker spectrometers

4 protocols using inova 600 mhz spectrometer

Structural Analysis of Mfp-6 Protein

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Nuclear magnetic resonance (NMR) spectroscopy was performed on a Varian Inova 600 MHz spectrometer or a Bruker Avance III Ultrashield 800 MHz spectrometer each equipped with a ¹H/¹³C/¹⁵N/²H four-channel cryoprobe for optimal ¹H detection. All experiments were conducted at 25 °C unless otherwise stated. The NMR sample contained various concentrations of proteins in 85% H₂O, 10% D₂O, and 5% d₄-acetic acid at pH 3. Water suppression was achieved with water flip-back¹⁸ and watergate^{19 (link)} techniques. NMR data were processed and analyzed with instrument software and the nmrPipe package.^{20 (link)} Nuclear Overhauser effect spectroscopy (NOESY) was performed with a mixing time of 150 or 180 ms. Quality controls applied to purified Mfp-6 prior to NMR analysis were (1) homogeneity determiined by SDS–PAGE, (2) mass homogeneity determined by MALDI-TOF mass spectrometry after multiple charge deconvolution (Figure S1D), and (3) no more than one disulfide bond determined by amino acid analysis.

Nicklisch S.C., Spahn J.E., Zhou H., Gruian C.M, & Waite J.H. (2016). Redox Capacity of an Extracellular Matrix Protein Associated with Adhesion in Mytilus californianus. Biochemistry, 55(13), 2022-2030.

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Validating Designed Protein Structures

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To confirm the core packing of designed proteins, we measured 2D ¹H-¹⁵N HSQC spectra for all designs that were monomeric and had the αβ-protein CD spectrum. The spectra were collected for 0.2–1.5 mM protein samples in 90% ¹H₂O/10% ²H₂O PBS buffer (pH 7.4) at 25 °C on a Varian INOVA 600 MHz spectrometer for the designs of Pl2×3_BP, R2×3_BP1_A, R2×3_BP1_B, R3×3_BP1, and R3×3_BP2, on a Bruker 800 MHz spectrometer for the designs of R2×3_BP4 and on a JEOL JNM-ECA 600 MHz spectrometer for the designs of R3×3_BP3, and were processed and analyzed using AutoProc/NMRpipe, Bruker TopSpin and JEOL Delta NMR software, respectively.

Koga N., Koga R., Liu G., Castellanos J., Montelione G.T, & Baker D. (2021). Role of backbone strain in de novo design of complex α/β protein structures. Nature Communications, 12, 3921.

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NMR Spectroscopy of 4E-BP1/eIF4E Complex

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We recorded all NMR spectra at 298 K on a Varian Inova 600 MHz spectrometer or a Bruker 750 MHz spectrometer, both equipped with cryogenic probes. We processed and analyzed the data using NMRPipe (Delaglio et al. 1995 (link)) and CARA (Keller 2004 ), respectively. We assigned the backbone chemical shifts of ¹⁵N¹³C4E-BP1_44–87 and ¹⁵N¹³C4E-BP1_44–87/eIF4E/m⁷GTP using TROSY versions of the traditional triple-resonance experiments: HNCA, HNCOCA, HNCO, HNCACO, HNCACB, and HNCOCACB. We deuterated all NMR observable samples except for 4E-BP1 alone. We used Non Uniform Sampling (NUS) in the two indirect dimensions to collect triple resonance data and used Poisson Gap Sampling to sample 12–15% of the indirect grid (Hyberts et al. 2010 (link)). We used the hmsIST program to reconstruct and process the data (Hyberts et al. 2012 (link)).

Sekiyama N., Boeszoermenyi A., Arthanari H., Wagner G, & Léger-Abraham M. (2017). 1H, 13C, and 15N backbone chemical shift assignments of 4E-BP144–87 and 4E-BP144–87 bound to eIF4E. Biomolecular NMR assignments, 11(2), 187-191.

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NMR Spectroscopy for Protein Structural Assignments

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All NMR experiments were carried out at 298 K on a Varian Inova 600 MHz spectrometer equipped with a 5 mm HCN cryogenic probe and a Bruker Avance III 850 MHz spectrometer equipped with a 5 mm HCN conventional room temperature probe. The collected NMR data included: 2D ¹H-¹⁵N HSQC, ¹H-¹³C HSQC, 3D HNCO, HN(CA)CO, HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CCO)NH, and C(CO)NH for backbone assignments, and 2D ¹H-¹³C HSQC (aliphatic and aromatic), 3D H(C)CH-TOCSY, H(C)CH-COSY, (H)CCH-TOCSY, and 4D CC NOESY for side chain assignments. The stereospecific assignments of isopropyl methyl groups of Val and Leu residues were determined from 2D constant-time ¹H-¹³C HSQC spectrum for the NC5 sample [33 (link)]. The data were processed using the NMRPipe [34 (link)] and analyzed with the Sparky program [35 (link)]. The backbone and side-chain resonances were automatically assigned using the PINE server from NMRFAM [36 (link)], and subsequently validated and corrected manually. All assignments were further confirmed from NOESY spectra, including 3D ¹⁵N-edited NOESY-HSQC and ¹³C-edited NOESY-HSQC. Chemical shift assignments have been deposited in the BioMagResBank (BMRB accession number 16688).

Shan Y., He X., Wang Z., Yue X., Zhu J., Yang Y, & Liu M. (2021). Structural Investigations on the SH3b Domains of Clostridium perfringens Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function. Molecules, 26(18), 5716.

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