NMR study of non-freezing water in protein-modified carbon adsorbents

T. A. Alekseeva, N. I. Lebovka, S. V. Mikhailovsky

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1 Citation (Scopus)


Temperature dependences of 1H NMR spin-spin relaxation were studied for the non-freezing water at the surface of carbon matrices modified with proteins (human serum albumin (HSA) and mouse immunoglobulin (MIG)) in the presence of water-soluble carbodiimide. The entropy, ΔS, and enthalpy, ΔH, values characterizing molecular mobility in non-freezing water were estimated. The compensation effect was observed for all modified samples, which is well approximated by the linear dependence of the type ΔH=T0Δ + ΔH0. The compensation temperature T0 = 231 ± 33 corresponds to such a state of non-freezing water, when the effect of modifying additives on the isobaric potential of molecular mobility activation in the non-freezing water, ΔG, is minimal. The ΔG has approximately constant value equal to ΔH0 = 24.2 ± 0.5 kJ/mol. Modification of the base carbon matrix with MIG protein results in higher structurization of the non-freezing water, whereas HSA reduces this structurization. The observed effects are explained in terms of the hydration of modifying agents and also by the peculiarities of their location on the surface of carbon adsorbent.

Original languageEnglish
Pages (from-to)275-279
Number of pages5
JournalColloid Journal
Issue number3
Publication statusPublished - 2003

ASJC Scopus subject areas

  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

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