A decrease in flexibility of mouse methionine-sulfoxide reductase B1 because of oxidation

Biophysics and medical physics

The spatial structure of mouse MsrBl protein in oxidized state has been determined with molecular mechanics and molecular dynamics computational methods and a possible mechanism of its oxidation has been analyzed. It was found that the disulphide bond formed upon protein oxidation, decreases flexibility of its polypeptide chain, excluding regions responsible for substrate binding and for interaction with tioredoxin.