title: Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins.
abstract: Significant non-reversible two-state denaturation was observed for proteins such as myoglobin (Mb) and α-chymotrypsin (CT) with decreasing temperature in the presence of 1-butyl-3-methylimidazolium-based ([C4mim](+)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.
authors: Department of Chemistry, University of Delhi, Delhi - 110 007, India. venkatesup@hotmail.com pvenkatesu@chemistry.du.ac.in.
authors: Awanish
authors: A
authors: Kumar
authors: Anjeeta
authors: A
authors: Rani
authors: Pannuru
authors: P
authors: Venkatesu
authors: Anil
authors: A
authors: Kumar
mesh_terms: D003080:Cold Temperature; D052578:Ionic Liquids; D058767:Protein Unfolding
chemical_list: D052578:Ionic Liquids