@article {44156,
	title = {Alternatively packed dry molten globule-like intermediate in the native state ensemble of a multidomain protein},
	journal = {Journal of Physical Chemistry B},
	volume = {121},
	year = {2017},
	month = {OCT},
	pages = {9336-9347},
	type = {Article},
	abstract = {It has been difficult to quantify the degree of side-chain conformational heterogeneity in the native (N) state ensemble of proteins and the relative energetic contributions of the side-chain packing and the hydrophobic effect in protein stability. Here, we show using multiple site specific spectroscopic probes and tools of thermodynamics that the N state ensemble of a multidomain protein contains an equilibrium intermediate (I) whose interdomain region resembles a dry molten globule. In the I state, a tryptophan residue in the interdomain region is alternatively packed, but its secondary structure and intradomain packing are N-like. The I state also has a larger interdomain distance, but the domain-domain interface is dry and molten. Our results indicate that hydrophobic desolvation and side-chain packing are decoupled during protein folding and that interdomain packing interactions have an important energetic contribution in protein stability. Dynamic interconversion between alternatively packed N-like states could be important for multiple allosteric and ligand binding functions of this protein.},
	doi = {10.1021/acs.jpcb.7b07032},
	author = {Mishra, Prajna and Jha, Santosh Kumar}
}
