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Study of Protein Structures under the Influence of Imidazolium Based Ionic Liquids: A Mini Review
Corresponding Author(s) : Anisur R. Molla
Asian Journal of Chemistry,
Vol. 34 No. 7 (2022): Vol 34 Issue 7, 2022
Abstract
Ionic liquids are nowadays extremely popular in the advanced research field of many disciplines including chemistry, chemical engineering, material science, biology and pharmaceuticals. Unique physico-chemical properties of the ionic liquids such as low vapor pressure, stability, large liquid range, broad solubility and easy modification of structures are responsible for its vast application. Imidazolium based ionic liquids are one of the most widely used ionic liquids and theses are extensively studied in the field of protein research. In this mini-review, imidazolium ionic liquid induced effect on the structure and function of protein molecules are discussed.
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K. Ghandi, Green Sustainable Chem., 4, 44 (2014); https://doi.org/10.4236/gsc.2014.41008
Z. Lei, B. Chen, Y. Koo and D.R. MacFarlane, Chem. Rev., 117, 6633 (2017); https://doi.org/10.1021/acs.chemrev.7b00246
K.S. Egorova, E.G. Gordeev and V.P. Ananikov, Chem. Rev., 117, 7132 (2017); https://doi.org/10.1021/acs.chemrev.6b00562
T.L. Greaves and C.J. Drummond, Chem. Rev., 115, 11379 (2015); https://doi.org/10.1021/acs.chemrev.5b00158
R. Jindal and A. Sablok, Curr. Green Chem., 2, 135 (2015); https://doi.org/10.2174/2213346101666140915212515
I. Jha and P. Venkatesu, Phys. Chem. Chem. Phys., 17, 20466 (2015); https://doi.org/10.1039/C5CP01735A
S. Mallakpour and M. Dinari, Eds.: A. Mohammad and D. Inamuddin, Ionic Liquids as Green Solvents: Progress and Prospects, In: Green Solvents II. Springer, Dordrecht (2012).
M. Watanabe, M.L. Thomas, S. Zhang, K. Ueno, T. Yasuda and K. Dokko, Chem. Rev., 117, 7190 (2017); https://doi.org/10.1021/acs.chemrev.6b00504
N.V. Plechkova and K.R. Seddon, Chem. Soc. Rev., 37, 123 (2008); https://doi.org/10.1039/B006677J
R. Patel, M. Kumari and A.B. Khan, Appl. Biochem. Biotechnol., 172, 3701 (2014); https://doi.org/10.1007/s12010-014-0813-6
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R.W. Newberry and R.T. Raines, ACS Chem. Biol., 14, 1677 (2019); https://doi.org/10.1021/acschembio.9b00339
R.L. Baldwin, Eds.: J. Buchner and T. Kiefhaber, Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds and Peptide Solvation, In: Protein Folding Handbook (2005).
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H. Weingärtner, C. Cabrele and C. Herrmann, Phys. Chem. Chem. Phys., 14, 415 (2012); https://doi.org/10.1039/C1CP21947B
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S. Saha J. Adv. Sci. Res., 12, 01 (2021).
T. Ku, P. Lu, C. Chan, T. Wang, S. Lai, P. Lyu and N. Hsiao, Comput. Biol. Chem., 33, 445 (2009); https://doi.org/10.1016/j.compbiolchem.2009.10.002
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S. Daneshjoo, N. Akbari, A.A. Sepahi, B. Ranjbar, R. Khavarinejad and K. Khajeh, Eng. Life Sci., 11, 259 (2011); https://doi.org/10.1002/elsc.201000154
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A.C. Salvador, M.C. Santos and J.A. Saraiva, Green Chem., 12, 632 (2010); https://doi.org/10.1039/b918879g
J.Q. Lai, Z. Li, Y.H. L¨u and Z. Yang, Green Chem., 13, 1860 (2011); https://doi.org/10.1039/c1gc15140a
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