Maintenance of native structure and function of the protein is a major concern for industrial production
of aggregation prone therapeutically important recombinant proteins. Aggregation may results due to
change in the native conformation of proteins under different stress conditions. To overcome the problem
of protein aggregation, role of silver and gold nanoparticles have been investigated. The nanoparticles
owing to their affirmative interaction with the proteins possess chaperoning activities and protect the
native state from denaturation. In the present study, through performing chemical denaturation of
zebrafish dihydrofolate reductase using denaturants like guanidine hydrochloride and urea in the
presence and absence of gold and silver nanoparticles and monitoring the process through enzyme
activity assay and intrinsic tryptophan fluorescence, we have demonstrated the impact of nanoparticles
in maintaining native conformation of proteins. Further, the outcome of refolding studies of DHFR
protein with nanoparticles monitored by UV-visible spectroscopy was also reported.