Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein
| Title | Dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein |
| Publication Type | Journal Article |
| Year of Publication | 2017 |
| Authors | Acharya, N, Mishra, P, Jha, SKumar |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 19 |
| Issue | 44 |
| Pagination | 30207-30216 |
| Date Published | NOV |
| Type of Article | Article |
| Abstract | The nature of the initial structural events during the base-induced unfolding of the native (N) state of proteins is poorly understood. Combining site-specific fluorescence resonance energy transfer, size exclusion chromatography, dynamic fluorescence quenching, red-edge excitation shift and circular dichroism spectroscopy, we show here that an early intermediate during the base-induced unfolding of a multidomain protein, i.e., the B form, has features of a dry molten globule. We show that the N (sic) B transition involves protein expansion and loosening of packing of inter-domain helices near domains I and II without the disruption of intra-domain packing or any change in hydration of the inter-domain region which resembles a molten hydrocarbon. Surprisingly, the disruption of inter-domain packing accounts for 40-45% of the total change in free energy of complete unfolding. Our results show that the disruption of van der Waals packing can be decoupled in different regions of a protein and could occur prior to hydrophobic solvation during base-induced unfolding, challenging the existing notion. |
| DOI | 10.1039/c7cp06614g |
| Type of Journal (Indian or Foreign) | Foreign |
| Impact Factor (IF) | 4.449 |
Divison category:
Physical and Materials Chemistry
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