References
- Ab Rani, M. A., Brant, A., Crowhurst, L., Dolan, A., Lui, M., Hassan, N. H., & Wilding, R. (2011). Understanding the polarity of ionic liquids. Physical Chemistry Chemical Physics, 13, 16831–16840. doi:10.1039/c1cp21262a
- Bukach, O. V., Glukhova, A. E., Seit-Nebi, A. S., & Gusev, N. B. (2009). Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20). Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics, 1794, 486–495. doi:10.1016/j.bbapap.2008.11.010
- Fedotoff, O., Mikheeva, L. M., Chait, A., Uversky, V. N., & Zaslavsky, B. Y. (2012). Influence of serum proteins on conformation of prostate-specific antigen. Journal of Biomolecular Structure and Dynamics, 29, 1051–1064. doi:10.1080/073911012010525030
- Ferreira, L. A., Breydo, L., Reichardt, C., Uversky, V. N., & Zaslavsky, B. Y. (2016). Effects of osmolytes on solvent features of water in aqueous solutions. Journal of biomolecular structure & dynamics, 35, 1055–1068. doi:10.1080/07391102.2016.1170633
- Ferreira, L. A., Cole, J. T., Reichardt, C., Uversky, V. N., Holland, N. B., & Zaslavsky, B. Y. (2015). Solvent properties of media in aqueous solutions of elastin-like polypeptide. International Journal of Molecular Sciences, 116, 13528–13547. doi:10.3390/ijms160613528
- Ferreira, L. A., Loureiro, J. A., Gomes, J., Uversky, V. N., Madeira, P. P., & Zaslavsky, B. Y. (2016). Why physicochemical properties of aqueous solutions of various compounds are linearly interrelated. Journal of Molecular Liquids, 221, 116–123. doi:10.1016/j.molliq.2016.05.068
- Ferreira, L. A., Madeira, P. P., Breydo, L., Reichardt, C., Uversky, V. N., & Zaslavsky, B. Y. (2016). Role of solvent properties of aqueous media in macromolecular crowding effects. Journal of Biomolecular Structure and Dynamics, 34, 92–103. doi:10.1080/07391102.2015.1011235
- Kamlet, M. J., Abboud, J. L., & Taft, R. W. (1977). The solvatochromic comparison method. 6. The .pi.* scale of solvent polarities. Journal of the American Chemical Society, 99, 6027–6038. doi:10.1021/Ja00460a031
- Kamlet, M. J., & Taft, R. W. (1976). The solvatochromic comparison method. I. The .beta.-scale of solvent hydrogen-bond acceptor (HBA) basicities. Journal of the American Chemical Society, 98, 377–383. doi:10.1021/Ja00418a009
- Kato, K., Goto, S., Inaguma, Y., Hasegawa, K., Morishita, R., & Asano, T. (1994). Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin. Journal of Biological Chemistry, 269, 15302–15309.
- Mymrikov, E. V., & Haslbeck, M. (2015). Medical implications of understanding the functions of human small heat shock proteins. Expert Review of Proteomics, 12, 295–308. doi:10.1586/14789450.2015.1039993
- Mymrikov, E. V., Seit-Nebi, A. S., & Gusev, N. B. (2011). Large potentials of small heat shock proteins. Physiological Reviews, 91, 1123–1159. doi:10.1152/physrev.00023.2010
- Sluchanko, N. N., Chebotareva, N. A., & Gusev, N. B. (2015). Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation. Biochimie, 108, 68–75. doi:10.1016/j.biochi.2014.11.001
- Taft, R. W., & Kamlet, M. J. (1976). Solvatochromic comparison method. 2. Alpha-scale of solvent hydrogen-bond donor (Hbd) acidities. Journal of the American Chemical Society, 98, 2886–2894. doi:10.1021/Ja00426a036
- Zaslavsky, A., Madeira, P., Breydo, L., Uversky, V. N., Chait, A., & Zaslavsky, B. (2013). High throughput characterization of structural differences between closely related proteins in solution. Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics, 1834, 583–592. doi:10.1016/j.bbapap.2012.11.004