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THz spectroscopy was used to investigate bovine serum albumin (BSA) flexibility in conditions ranging from lyophilised BSA to dilute 10% w/w BSA solution and highly concentrated 50% w/w BSA solutions. The simulated THz spectra of dry and hydrated BSA are in good agreement with the experiments.
THz spectroscopy is a very powerful tool in investigating the vibrational modes and conformational transitions of biomolecules. Here we have used THz spectroscopy to study the vibrational spectrum of bovine serum albumin, a protein whose 3D structure is yet unknown. Experimental data were fitted with theoretical spectra obtained by normal modes analysis of BSA structures generated by homology modeling.
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