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  Unexpected Trends in the Hydrophobicity of Fluorinated Amino Acids Reflect Competing Changes in Polarity and Conformation

Robalo, J. R., & Vila Verde, A. (2019). Unexpected Trends in the Hydrophobicity of Fluorinated Amino Acids Reflect Competing Changes in Polarity and Conformation. Physical Chemistry Chemical Physics, 21(4), 2029-2038. doi:10.26434/chemrxiv.7442648.v1.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-AC4B-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-3419-7
Genre: Journal Article

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Robalo, João Ramiro1, 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: Fluorination can dramatically improve the thermal and proteolytic stability of proteins and their enzymatic activity. Key to the impact of fluorination on protein properties is the hydrophobicity of fluorinated amino acids. We use molecular dynamics simulations, together with a new fixed-charge, atomistic force field, to quantify the changes in hydration free energy, DGHyd , for amino acids with alkyl side chains and with 1 to 6 –CH!–CF side chain substitutions. Fluorination changes DGHyd by −1.5 to +2 kcal mol−1, but the number of fluorines is a poor predictor of hydrophobicity. Changes in DGHyd reflect two main contributions: i) fluorination alters side chain-water interactions; we identify a crossover point from hydrophilic to hydrophobic fluoromethyl groups which may be used to estimate the hydrophobicity of fluorinated alkyl side-chains; ii) fluorination alters the number of backbone-water hydrogen bonds via changes in the relative side chain-backbone conformation. Our results offer a road map to mechanistically understand how fluorination alters hydrophobicity of (bio)polymers.

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 Dates: 2018-12-1020182019
 Publication Status: Published in print
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Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
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Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 21 (4) Sequence Number: - Start / End Page: 2029 - 2038 Identifier: ISSN: 1463-9076