thiolation

the protein underwent rapid thiolation after exposure to the reducing agent.

thiolation of cysteine residues is crucial for enzyme activity in some cases.

we observed significant thiolation during the protein folding process.

the researchers investigated the role of thiolation in peptide aggregation.

thiolation can be used to modify protein surfaces for bioconjugation.

the extent of thiolation was quantified using a thiol-specific dye.

reversible thiolation provides a mechanism for redox regulation of proteins.

thiolation patterns differ between the wild-type and mutant protein.

site-specific thiolation was achieved using a targeted chemical modification.

the impact of thiolation on protein stability was assessed experimentally.

we are studying the kinetics of thiolation under various conditions.