Affiliations: Faculty of Physics and International Laser Center, Moscow State University, Leninskie Gory, Moscow, Russia | Faculty of Bioengineering and Bioinformatics, Moscow State University, Leninskie Gory, Moscow, Russia
Note: [] Corresponding author: V.N. Kruzhilin, Faculty of Physics and International Laser Center, Moscow State University, Leninskie Gory, 119991, GSP-1, Moscow, Russia. E-mail: [email protected]
Abstract: Disulfide bridges of bovine α-thrombin are studied using the analysis of the Raman spectral features in the spectral interval 500–550 cm−1. The changes under study are caused by the transitions from lyophilized state to the native solution in PBS with a protein concentration of 2.8 mM (100 mg/ml) and from native solution to solution with partially reduced disulfide bridges. The reduction takes place when dithiothreitol (DTT) is added to the sample.