<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kumar, Awanish</style></author><author><style face="normal" font="default" size="100%">Rani, Anjeeta</style></author><author><style face="normal" font="default" size="100%">Venkatesu, Pannuru</style></author><author><style face="normal" font="default" size="100%">Kumar, Anil</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins</style></title><secondary-title><style face="normal" font="default" size="100%">Physical Chemistry Chemical Physics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">30</style></number><publisher><style face="normal" font="default" size="100%">ROYAL SOC CHEMISTRY</style></publisher><pub-location><style face="normal" font="default" size="100%">THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">16</style></volume><pages><style face="normal" font="default" size="100%">15806-15810</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">30</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.68</style></custom4></record></records></xml>