Infrared spectroscopy (including far infrared) covers the vibration, rotation and energy transition of molecular interactions of biological macromolecules (such as proteins, nucleic acids, sugars, lipids, etc.), and therefore becomes a powerful tool for analyzing the chemical composition of biological samples. When using high-brightness synchrotron radiation for infrared microscopy and imaging research, high spatial resolution of the theoretical diffraction limit can be achieved, and infrared spectra with high intensity and signal-to-noise ratio can still be obtained when the aperture size is 5μm×5μm, overcoming the shortcomings of the traditional FTIR spectrometer light source with weak signal, poor signal-to-noise ratio and low spatial resolution under the small aperture.
Synchrotron radiation infrared spectroscopy can be applied to the analysis of many types of samples in biomedicine, pharmaceutical chemistry, chemistry, materials, environmental science and other fields. Meanwhile, the infrared time-resolved experimental station can detect the physical changes of structure and spatial morphology during the dynamic process of sample points. The time scale of the infrared spectral transition is picosecond, which is much smaller than that of nuclear magnetic resonance analysis, so it has the potential to study the time-resolved molecular structure dynamics.
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