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Binding Energetics of Lysozyme to Copolymers of N ‐Isopropylacrylamide with Sodium Sulfonated Styrene
Author(s) -
Burova Tatiana V.,
Grinberg Natalia V.,
Grinberg Valerij Ya.,
Tang Yecang,
Zhang Guangzhao,
Khokhlov Alexei R.
Publication year - 2009
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200800313
Subject(s) - copolymer , lysozyme , polymer chemistry , differential scanning calorimetry , chemistry , styrene , ionic strength , macromolecule , polymer , polyelectrolyte , crystallography , organic chemistry , aqueous solution , biochemistry , thermodynamics , physics
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.