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Issue 44, 2017
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A dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein

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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 ⇌ 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.

Graphical abstract: A dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein

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Publication details

The article was received on 27 Sep 2017, accepted on 27 Oct 2017 and first published on 27 Oct 2017


Article type: Paper
DOI: 10.1039/C7CP06614G
Citation: Phys. Chem. Chem. Phys., 2017,19, 30207-30216
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    A dry molten globule-like intermediate during the base-induced unfolding of a multidomain protein

    N. Acharya, P. Mishra and S. K. Jha, Phys. Chem. Chem. Phys., 2017, 19, 30207
    DOI: 10.1039/C7CP06614G

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