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  Proteins maintain hydration at high [KCl] concentration regardless of content in acidic amino acids

Geraili Daronkola, H., & Vila Verde, A. (2021). Proteins maintain hydration at high [KCl] concentration regardless of content in acidic amino acids. Biophysical Journal, 120(13), 2746-2762. doi:10.1016/j.bpj.2021.05.015.

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Geraili Daronkola, Hosein1, Author              
Vila Verde, Ana1, Author              
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1Ana Vila Verde, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2205638              

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 Abstract: Proteins of halophilic organisms, which accumulate molar concentrations of KCl in their cytoplasm, have a much higher content in acidic amino acids than proteins of mesophilic organisms. It has been proposed that this excess is necessary to maintain proteins hydrated in an environment with low water activity, either via direct interactions between water and the carboxylate groups of acidic amino acids or via cooperative interactions between acidic amino acids and hydrated cations. Our simulation study of five halophilic proteins and five mesophilic counterparts does not support either possibility. The simulations use the AMBER ff14SB force field with newly optimized Lennard-Jones parameters for the interactions between carboxylate groups and potassium ions. We find that proteins with a larger fraction of acidic amino acids indeed have higher hydration levels, as measured by the concentration of water in their hydration shell and the number of water/protein hydrogen bonds. However, the hydration level of each protein is identical at low (bKCl = 0.15 mol/kg) and high (bKCl = 2 mol/kg) KCl concentrations; excess acidic amino acids are clearly not necessary to maintain proteins hydrated at high salt concentration. It has also been proposed that cooperative interactions between acidic amino acids in halophilic proteins and hydrated cations stabilize the folded protein structure and would lead to slower dynamics of the solvation shell. We find that the translational dynamics of the solvation shell is barely distinguishable between halophilic and mesophilic proteins; if such a cooperative effect exists, it does not have that entropic signature.

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Language(s): eng - English
 Dates: 2021-07-022021
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1016/j.bpj.2021.05.015
BibTex Citekey: GERAILI2021
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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 120 (13) Sequence Number: - Start / End Page: 2746 - 2762 Identifier: ISSN: 0006-3495