Students/Projects Trainees

Former Students/Projects Trainees

Complete list of publications -Google scholar: https://scholar.google.com/citations?user=stWgX-cAAAAJ&hl=en 

Functional proteins emerge as a consequence of a complex folding pathways. Mutations in the wild type gene sequence can result in a failure to acquire native conformation and is the underlying cause of protein misfolding and diseases like cancers and neurodegeneration. Interestingly, mutations can also revert pathological conditions and might confer advantage to the organism like prions or amyloid form of proteins serve as environmental shields forming biofilms, long-term memory acquisition, and drug resistance. Hence the functional space of proteins is much larger than anticipated by natively acquired conformations and unexplored for translational benefits. Our lab is deeply interested in exploring the sequence space of proteins to identify novel mutations with improved functions. We are currently focusing on exploring the escape mutants in aggregation of prion protein, synuclein and ataxin along with their regulatory protein, ubiquitin. The conformational changes in the mutant form of our target proteins can sculpt phenotypic landscapes as well as shape evolutionary processes. We employ high throughput mutagenesis, protein engineering and genetic manipulations in the unicellular eukaryote Saccharomyces cerevisiae (baker's yeast) as the host organism to investigate

(1) Dominant negative mutations to reveal critical protein-protein interactions

(2) Mutations with anti-aggregation phenotypes in amyloid proteins

(3) Mutations that inhibit enzymatic functions particularly of disease relevant deubiquitinases.

Yeast serve as a powerful unicellular eukaryote for unbiased high-throughput screening of mutations. The mutant proteins screened with desired phenotypes are further studied by a combination of biochemical and biophysical methods to uncover mechanistic details of their functions.

We are motivated to identify the cryptic/novel mutations in proteins which for multi-functional proteins can affect only desired interactions or can reverse the toxic oligomers of misfolded proteins to counteract the enigmatic disease conditions.

For a trainee opportunity in our lab, please contact at pmsl@uohyd.ac.in

We encourage applications from highly motivated students and appreciate the applicant to write the aspects of our research that interests them to work with us. We welcome CSIR, UGC, ICMR or DBT fellowship holders as well as non-fellowship holders for PhD positions available through the University of Hyderabad PhD program. Application enclosing a CV, research interests and two references for evaluation should be sent by the prospective candidate.