Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects

P. Tompa, P. Bánki, M. Bokor, P. Kamasa, D. Kovács, G. Lasanda, K. Tompa

Research output: Contribution to journalArticle

88 Citations (Scopus)

Abstract

Proton NMR intensity and differential scanning calorimetry measurements were carried out on an intrinsically unstructured late embryogenesis abundant protein, ERD10, the globular BSA, and various buffer solutions to characterize water and ion binding of proteins by this novel combination of experimental approaches. By quantifying the number of hydration water molecules, the results demonstrate the interaction between the protein and NaCl and between buffer and NaCl on a microscopic level. The findings overall provide direct evidence that the intrinsically unstructured ERD10 not only has a high hydration capacity but can also bind a large amount of charged solute ions. In accord, the dehydration stress function of this protein probably results from its simultaneous action of retaining water in the drying cells and preventing an adverse increase in ionic strength, thus countering deleterious effects such as protein denaturation.

Original languageEnglish
Pages (from-to)2243-2249
Number of pages7
JournalBiophysical journal
Volume91
Issue number6
DOIs
Publication statusPublished - 2006

ASJC Scopus subject areas

  • Biophysics

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