A new study has shed light on the role of oxidized tryptophan (Trp) residues in proteins. Scientists from the Institute of Molecular Biotechnology (IMBA) in Austria have characterized the oxidation state of Trp residues in proteins, allowing them to better understand their role in protein folding and stability.

The scientists studied the oxidation state of Trp residues in several proteins, and found that oxidation of the Trp residues impaired protein folding and stability. They also found that Trp residues with different oxidation states had different effects on protein folding, suggesting that oxidation of Trp residues can be used to modulate protein structure and stability.

This new research provides an important insight into the role of oxidized Trp residues in proteins, and could open up new avenues for manipulating protein structure and stability.

Read Full Article Here

source: Phys.org