Hofmeister Ion-Induced Changes in Water Structure Correlate with Changes in Solvation of an Aggregated Protein Complex

Taylor Light, Karen Corbett, Michael Metrick, Gina MacDonald

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)


RecA is a naturally aggregating Escherichia coli protein that catalyzes the strand exchange reaction utilized in DNA repair. Previous studies have shown that the presence of salts influence RecA activity, aggregation, and stability and that salts stabilize RecA in an inverse-anionic Hofmeister series. Here we utilized attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy and circular dichroism (CD) to investigate how various Hofmeister salts alter the water structure and RecA solvation and aggregation. Spectroscopic studies performed in water and deuterium oxide suggest that salts alter water O-1H and O-2H stretch and bend vibrations as well as protein amide I (or I′) and amide II (or II′) vibrations. Anions have a much larger influence on water vibrations than cations. Water studies also show increased water-water and/or water-ion interactions in the presence of strongly hydrated SO42- salts and evidence for decreased interactions with weakly hydrated Cl- and ClO4- salts. Salt-water difference infrared spectra show that kosmotropic salts are more hydrated than chaotropic salts. Interestingly, this is the opposite trend to the changes in protein solvation. Infrared spectra of RecA show that vibrations associated with protein desolvation were observed in the presence of SO42- salts. Conversely, vibrations associated with protein solvation were observed in the presence of Cl- and ClO4- salts. Difference infrared studies on the dehydration of model proteins aided in identifying changes in RecA-solvent interactions. This study provides evidence that salt-induced changes in water vibrations correlate to changes in protein solvent interactions and thermal stability.

Original languageEnglish
Pages (from-to)1360-1369
Number of pages10
Issue number5
Publication statusPublished - 9 Feb 2016
Externally publishedYes

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