Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins
Literature Information
Awanish Kumar, Anjeeta Rani, Pannuru Venkatesu, Anil Kumar
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.
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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.










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![Bis(N,N''-dimethylpiperazine)tetra[copper(I) iodide] structure Bis(N,N''-dimethylpiperazine)tetra[copper(I) iodide] structure](https://static.chemtradehub.com/structs/140/1401708-91-5-2b86.webp)


