Supporting data for: Observation of High-Temperature Macromolecular Confinement in Lyophilised Protein Formulations Using Terahertz Spectroscopy
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All data that was used for the experiments reported in the linked publication. This includes data from circular dichroism measurements, differential scanning calorimetry, Fourier transform mid infrared analysis, solid state nuclear magnetic resonance spectroscopy and terahertz time-domain spectroscopy. See the Readme file for a detailed description.
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terahertz spectroscopy, infrared spectroscopy, ssNMR, DSC, lyophilisation, biopharmaceuticals, mAb, BSA, protein formulation, drug delivery, secondary structure, freeze drying, formulation stability, vibrational dynamics
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EPSRC (1198)