The World Academy of Sciences (TWAS) selected NCBS Senior Professor Jayant Udgaonkar to be a Fellow of the prestigious academy on October 2^nd, 2013. Membership to the Academy is based on scientific merit, and Udgaonkar is one of the 52 members to be appointed this year. "It's always nice to get recognition of this sort," says Udgaonkar. "It is motivating for both myself and my students." Udgaonkar will be inducted into the Academy at its 25^th General Meeting in 2014.

TWAS, an international science academy, was established in 1984 to promote science and engineering in the developing world. Members are elected for life, the main criteria being adherence to the highest international standards of research and scientific excellence.

And Udgaonkar's work on proteins can truly be described as the epitome of excellence. Proteins are large bio-molecules indispensable to most biological processes - from enabling responses to external stimuli such as heat, to acting as catalysts for chemical processes such as cell communication. Each functionally different protein has a unique structure. But how are these structures formed? Just like beads in a necklace, residues of amino acids fuse together to form what is known as a polypeptide chain. This chain folds, twists and turns to create a specific structure: the final functional protein. It is this intriguing phenomenon of folding, as well as unfolding and misfolding, that Udgaonkar's research focuses on. Understanding these complex phenomena brings science closer to unraveling the dynamics of health conditions such as Alzheimer's disease which are primarily due to faulty protein formation or misfolding.

Teasing out the specifics is therefore undeniably vital and Udgaonkar's research has thrown new light on crucial concepts. Udgaonkar's earlier work showed that protein folding begins by a collapse reaction - a sudden compaction of the unfolded protein - and that the protein's structure forms much later. Using experiments, Udgaonkar and his colleagues also showed that proteins can fold in multiple ways and are not restricted by any single pattern of folding. "We've shown that in a variety of different cases over the last 15-20 years," he says.

The last steps in the process of protein folding are akin to the initial stages of protein-unfolding, says Udgaonkar - a link that drew him to study unfolding as well. In 2008, Udgaonkar along with doctoral student Santhosh Kumar Jha demonstrated that the process of protein unfolding is a slow diffusive process, contrary to what previous studies had shown. The next year, they provided the first ever experimental evidence validating the presence of a new initial stage in the 'dry molten globule hypothesis', one of the elemental concepts that describe how proteins unfold. Research had already established that proteins first unfold to form a globule-shaped structure, and water molecules penetrate its core. Udgaonkar's team proved that water molecules do not penetrate the globule core in the initial phase - this happens only in the second, 'wet globule' phase. "Our work revolutionized the field and changed the way we think about protein stability," admits Jha.

"We're lucky that we could identify the dry molten globule state, which other people had not really been able to see for the last 15 years or so," says Udgaonkar. "Recently, we (Saswata Sarkar, G Krishnamoorthy and I) have got even better evidence for both dry and wet molten globules, which will be published this month." Udgaonkar and his team also plan to publish more case studies demonstrating the sequence of dry and wet globule formation using a range of different methodologies.

Udgaonkar's lab also works on the phenomenon of protein misfolding which leads to protein aggregation in cells, causing many diseases. "We have been studying various proteins including the prion protein associated with prion diseases, tau associated with Alzheimer's and the α-synuclein associated with Parkinson's," he says.

With such academically brilliant pursuits, fellowships to renowned academies are hardly a surprise. Udgaonkar is also a Fellow of the Indian National Science Academy and the Indian Academy of Sciences. His other eminent awards include the B.M. Birla Award for Biology in 1996, the Shanti Swarup Bhatnagar Award in 2000 and the G.N. Ramachandran Gold Medal from the Council of Scientific and Industrial Research in 2011. Udgaonkar feels that such recognition of his work has been helpful. "These kinds of awards are like milestones," he says. "It's not something you go after - but when you get it, you feel happy about it. It also makes the people around you happy, the people who matter: family and friends." His students are also elated at his election into the TWAS. "I am very happy that Jayant is part of this renowned academy because of his outstanding contributions to protein folding," says Sabareesan A.T., a Research Scholar in Udgaonkar's lab, a sentiment his former student Jha echoes. "It was great working with Jayant for my doctoral degree," says Jha. "He has been an excellent mentor and helped me realize my full potential. He has been very supportive, encouraging me to venture into uncharted territories of science."

Udgaonkar believes that awards like the TWAS Fellowship are also a recognition of his students' work, and appreciation for the entire laboratory. "It's a recognition of their ability to work at a level which is comparable to their peers anywhere else in the world," he says.

Apart from the recognition, does the Fellowship open up opportunities for interactions with other TWAS Fellows? "That will really be a major attraction," answers Udgaonkar. "When you meet and interact with other Fellows, you get a broader, more worldly perspective on what is happening in other countries."

Visit this link for more information on Jayant Udgaonkar's work at NCBS.