Article
A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties.
Scientific reports - 17 Dec 2013
Sharma Sunny, Sarkar Suparna, Paul Simanta Sarani, Roy Syamal, Chattopadhyay Krishnananda
Abstract excerpt
Protein aggregation is believed to occur through the formation of misfolded conformations. It is expected that, in order to minimize aggregation, an effective small molecule chaperone would destabilize these intermediates. To study the mechanism of a chemical chaperone, we have designed a series of mutant proteins in which a tryptophan residue experiences different local environments and solvent exposures. We...
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