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Binding Energetics of Lysozyme to Copolymers of N‐Isopropylacrylamide with Sodium Sulfonated Styrene |
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| Authors: | Tatiana V. Burova Natalia V. Grinberg Valerij Ya. Grinberg Yecang Tang Guangzhao Zhang Alexei R. Khokhlov |
| Affiliation: | 1. A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Vavilov St. 28, 119991, Moscow, Russian Federation;2. N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Vavilov St. 28, Moscow, Russian Federation;3. Department of Chemical Physics, University of Science and Technology of China, Heifei, China;4. Department of Physics, M.V. Lomonosov Moscow State University, Moscow, Russian Federation |
| Abstract: | Interpolyelectrolyte complexes of lysozyme with thermosensitive N‐isopropylacrylamide–sodium sulfonated styrene copolymers of different charge density were investigated by high‐sensitivity differential scanning calorimetry (HS‐DSC) at pH 4.6–7.2 and low ionic strength. A general property of the complexes for all copolymers investigated was a decrease in the conformational stability of the bound protein. This suggested the preferential binding of the unfolded protein to the polymer matrix. The isotherms of lysozyme binding to the copolymers were derived from the HS‐DSC data. They indicate that the binding is irreversible and charge stoichiometric.  |
| Keywords: | differential scanning calorimetry interpolyelectrolyte complexes order‐disorder transitions polyelectrolytes proteins protein denaturation thermodynamics |