Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 118; no. 34; pp. 1 - 9
• Main Authors: Okuno, Yusuke, Yoo, Janghyun, Schwieters, Charles D., Best, Robert B., Chung, Hoi Sung, Clore, G. Marius
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 24.08.2021
• Subjects: Animals; Biological Sciences; Biopolymer denaturation; Destabilization; Drosophila melanogaster; Drosophila Proteins - chemistry; Drosophila Proteins - metabolism; Electrostatic properties; Equilibrium; Models, Molecular; NMR; Nuclear magnetic resonance; Physical Sciences; Protein Denaturation; Protein Folding; Protein interaction; Protein Unfolding; Proteins; Solvents; Solvents - chemistry; src Homology Domains; Thermodynamics; drkN SH3 native and unfolded states; protein–cosolute interactions; transient states; NMR relaxation; replica exchange molecular dynamics

The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein st...