@article { ISI:000339628400010,
	title = {Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins},
	journal = {Physical Chemistry Chemical Physics},
	volume = {16},
	number = {30},
	year = {2014},
	month = {JUN},
	pages = {15806-15810},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>Significant non-reversible two-state denaturation was observed for proteins such as myoglobin (Mb) and alpha-chymotrypsin (CT) with decreasing temperature in the presence of 1-butyl-3-methylimidazolium-based ([C(4)mim]X-+(-)) ionic liquids (ILs) with various anions (X-). Interestingly, for the first time, ILs having acetate and bromide anions were proven to counteract the cold-induced unfolding of proteins.</p>},
	issn = {1463-9076},
	doi = {10.1039/c4cp01001a},
	author = {Kumar, Awanish and Rani, Anjeeta and Venkatesu, Pannuru and Kumar, Anil}
}
