Optical rotation data were obtained on a Rudolph Research AUTOPOL® III automatic polarimeter. ECD data were obtained on a JASCO J-715 CD instrument. NMR data were collected on Varian 500 and 600 MHz NMR spectrometers. Intensity data were collected using a D8 Quest κ-geometry diffractometer with a Bruker Photon II cmos area detector and an Incoatec Iμs microfocus Mo Kα source (λ = 0.71073 Å). LC-MS data were obtained on a Shimadzu LC-MS 2020 system (ESI quadrupole) coupled to a photodiode array detector, with a Phenomenex Kintex 2.6 μm C18 column (100 Å, 75 × 3.0 mm, 0.4 mL/min). The preparative HPLC system utilized SCL-10A VP pumps and system controller with Phenomenex Gemini 5 μm C18 column (110 Å, 250 × 21.2 mm, 10 mL/min), the analytical and semi-preparative HPLC system utilized Waters 1525 binary pumps with Waters 2998 photodiode array detectors, and Phenomenex Gemini 5 μm Gemini C18, Phenomenex Kinetex 5 μm biphenyl, Phenomenex Kinetex 5 μm pentafluorophenyl (250 × 4.6 mm, 1 mL/min and 250 × 10 mm, 4 mL/min). Accurate mass data were collected on a Waters SYNAPT G2-Si mass spectrometer. All solvents were of ACS grade or better.
J 715 cd instrument
Manufactured by Jasco
Sourced in Japan
The J-715 CD instrument is a compact and versatile circular dichroism spectrometer designed for a wide range of applications. It measures the differential absorption of left and right circularly polarized light by chiral molecules, providing insights into the structural properties of proteins, nucleic acids, and other biomolecules.
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2 protocols using j 715 cd instrument
1
Comprehensive Analytical Characterization
2
Biophysical Characterization of Protein Samples
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All protein samples, except the peptide samples, were prepared using a buffer (pH 6.5, 50 mm MES, 50 mm NaCl, 5 µm ZnSO4, and 1 mm TCEP) through dialysis or SEC. ITC experiments were performed using the Auto‐iTC200 micro‐calorimeter (Malvern Panalytical, Malvern, UK) at 10 °C. The low concentrated protein was loaded in the sample cell, and 15–30 higher concentrated titrant protein was placed in the syringe. ITC data were analysed using the microcal origin ™ software.
Circular dichroism spectra were recorded using the J‐715 CD instrument (JASCO, Tokyo, Japan) with 0.05 cm path‐length circular CD cell to measure high‐concentration protein samples (0.1 mm , > 3.0 mg·mL−1). All protein and peptide samples were prepared using a buffer (pH 6.5, 50 mm MES, 50 mm NaCl, and 5 µm ZnSO4).
Circular dichroism spectra were recorded using the J‐715 CD instrument (JASCO, Tokyo, Japan) with 0.05 cm path‐length circular CD cell to measure high‐concentration protein samples (0.1 m
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