@article {46196,
	title = {Slow motion protein dance visualized using red-edge excitation shift of a buried fluorophore},
	journal = {Journal of Physical Chemistry B},
	volume = {123},
	year = {2019},
	month = {FEB},
	pages = {1256-1264},
	type = {Article},
	abstract = {<p>It has been extremely challenging to detect protein structures with a dynamic core, such as dry molten globules, that remain in equilibrium with the tightly packed native (N) state and that are important for a myriad of entropy-driven protein functions. Here, we detect the higher entropy conformations of a human serum protein, using red-edge excitation shift experiments. We covalently introduced a fluorophore inside the protein core and observed that in a subset of native population, the side chains of the polar and buried residues have different spatial arrangements than the mean population and that they solvate the fluorophore on a timescale much slower than the nanosecond timescale of fluorescence. Our results provide direct evidence for the dense fluidity of protein core and show that alternate side-chain packing arrangements exist in the core that might be important for multiple binding functions of this protein.</p>
},
	issn = {1520-6106},
	doi = {10.1021/acs.jpcb.8b11151},
	author = {Mishra, Prajna and Jha, Santosh Kumar}
}
