Abstract
In biomedicine and biophysics, the discrimination of protein conformations is of critical importance for identifying the unfolding states in the diagnosis of neurodegenerative diseases. We develop a dynamic Raman spectroscopic approach based on a statistical analysis of the time series of spectral fingerprints of single protein. We show that the unfolded state of bovine serum albumin can be identified in the time series using the fluctuations of the Raman bands of some amino acids, tryptophan, tyrosine, leucine, and histidine, acting as biomarkers. The statistical analysis induces also the sorting between physisorption and chemisorption events. This is confirmed by the spectral analysis of the different characteristic spectra highlighted based on the amino acids fingerprints following, notably, the hydrophobicity
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