Prokaryotic Chaperonins / Heat Shock Proteins Bd.11 (PDF)

C. M. Santosh Kumar started his research career as a molecular geneticist, exploring the functions of molecular chaperones in health and disease. His research aims at understanding the functions of the bacterial chaperonins, especially those of the multiple chaperonins. He has demonstrated that activity of a mycobacterial chaperonin is regulated by a phosphorylation switch that facilitates oligomerization. His current interests include unravelling the role of mycobacterial chaperonins in the establishment and progression of tubercular disease.








Shekhar C. Mande is a structural biologist interested in understanding the molecular attributes of mycobacterial stress proteins. He started his career as a structural biologist in understanding the structural features of peanut lectin. Further, he became interested in the structure-function relations of mycobacterial stress proteins, such as the redox proteins and heat-shock proteins. He led the way towards the understanding of structural features of the mycobacterial chaperonin proteins. His work demonstrated that mycobacterial chaperonins exhibit non-canonical attributes that are evolved to assist the pathogen in its disease establishment and progression. Concurrently, he began to explore the system wide functional interactions among the mycobacterial proteins. These investigations have led to the identification of several novel interactions that are currently being examined.