Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 11, Issue 11, Pages 4353-4358Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.0c00982
Keywords
-
Categories
Funding
- National Institute of General Medical Sciences of the National Institutes of Health [R01GM118774]
Ask authors/readers for more resources
Solvent-protein interactions are important for protein biological functions, especially for a coupled folding and binding system such as insulin. By monitoring the change in the conformation of insulin dimers during dissociation with temperature-jump infrared spectroscopy, we show that co-solvents can significantly destabilize the dimers by perturbing their hydrophobic center. The transition from the native to intermediate dimer state is observed as the buried residues are exposed to solvents in the presence of 10% dimethyl sulfoxide and with alpha-helices unfolding when ethanol is present, which reduces the dissociation time dramatically to 50% and 20% of the value in a D2O solution, respectively. We propose a self-consistent analysis using complementary methods to resolve this coupled folding and binding process and obtain a much higher rate of monomer association than of intermediate folding. Our results demonstrate that the conformational changes are critical in dimer formation and strongly affected by co-solvents.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available