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Investigates protein detection using quantum spectroscopy in biomolecular diagnostics, suggesting new design rules.
We investigate numerical modelling of quantum spectroscopy with undetected photons for protein detection in the mid-infrared spectral region. Classical Fourier-transform infrared spectroscopy of protein samples (bovine serum albumin and N-terminal pro-brain natriuretic peptide) is used as reference to define the sample’s mid-infrared absorption, which is then embedded in a numerical model of a double-pass quantum interferometer. We analyse parameters that influence visibility of the interference pattern formed by the signal beams, including the length of nonlinear crystal, sample length and mirror-sample distance. This leads us to a practical quantum spectrometer design with optimal image contrast at the specific amide I-II spectral bands. The simulated visibility spectra reproduce nearly identically the protein absorption features in the mid-IR and reveal temperature-induced changes to the protein secondary structure. Overall, this provides practical design rules for future quantum bio-spectroscopy applications that use only visible wavelength sources and detectors.
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Mohammadi et al. (2026) studied this question.
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