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

TitleProtein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects.
Publication TypeJournal Article
Year of Publication2006
AuthorsTompa, P., P. Bánki, M. Bokor, P. Kamasa, D. Kovacs, G. Lasanda, and K. Tompa
JournalBiophys J
Volume91
Issue6
Pagination2243-9
Date Published2006 Sep 15
ISSN0006-3495
KeywordsArabidopsis Proteins, Buffers, Calorimetry, Differential Scanning, Nuclear Magnetic Resonance, Biomolecular, Plant Proteins, Serum Albumin, Bovine, Sodium Chloride, Water
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.

DOI10.1529/biophysj.106.084723
Alternate JournalBiophys. J.
PubMed ID16798808
PubMed Central IDPMC1557563