When eukaryotic or unstable proteins are overexpressed in bacteria, these often form insoluble aggregates called inclusion bodies (IB). Refolding the proteins from inclusion bodies can be challenging, resulting in low ...

The unique native structure is a basic requirement for normal functioning of most proteins. Many diseases stem from mutations in proteins that destabilize the protein structure thereby resulting in impairment or loss of ...

Aminoacyl-tRNA synthetases (aaRSs) are at the center of the question of the origin of life and are essential proteins found in all living organisms. AARSs arose early in evolution to interpret genetic code and are believed ...

Native states of globular proteins typically show stabilization in the range of 5 to 15 kcal/mol with respect to their unfolded states. There has been a considerable progress in the area of protein stability and folding ...

Influenza virus is a pleiomorphic human pathogen which causes self-limiting respiratory illness lasting one-two weeks in most individuals. However, in immunologically compromised individuals, influenza infection may lead ...

Analyses of protein sequences from diverse genomes have revealed the ubiquitous nature of multi-domain proteins. They form up to 70% of proteomes of most eukaryotic organisms. Yet, our understanding of protein structure, ...

The thesis entitled “Folding studies on Peanut Agglutinin: A lectin with an unusual quaternary structure” deals with the several aspects of the folding of the tetrameric legume lectin Peanut Agglutinin ...