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The unfolding transition state of ubiquitin with charged residues has higher energy than that with hydrophobic residues

Phys Chem Chem Phys. 2020; 
Tathagata Nandi, Amogh Desai, Sri Rama Koti Ainavarapu
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Mutagenesis Services … energetics of ubiquitin. Experimental. Protein preparation and purification. The mutants without tryptophan were outsourced to GenScript Biotech Corp, through Biotech Desk Pvt. Ltd, India, in the vector pQE80L. Site directed … Get A Quote

摘要

The native-state structure and folding pathways of a protein are encoded in its amino acid sequence. Ubiquitin, a post-translational modifier, primarily noted for its role in intracellular protein degradation, has two salt bridges: one relatively exposed (SB1:K11-E34) and the other relatively buried (SB2:K27-D52). Here, we study the role of hydrophobic interactions and sequence specificity in protein folding, by mutating the salt-bridge residues in ubiquitin with hydrophobic residues. Equilibrium chemical denaturation using GdnHCl shows that the SB1 null variant is thermodynamically stabilised whereas the SB2 null variant is destabilised only slightly. The thermodynamic stability of the double salt-bridge (DB) ... More

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