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@ARTICLE{ElHarrar:916528,
      author       = {El Harrar, Till and Gohlke, Holger},
      title        = {{C}umulative {M}illisecond-{L}ong {S}ampling for a
                      {C}omprehensive {E}nergetic {E}valuation of {A}queous
                      {I}onic {L}iquid {E}ffects on {A}mino {A}cid {I}nteractions},
      journal      = {Journal of chemical information and modeling},
      volume       = {63},
      number       = {1},
      issn         = {0095-2338},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2022-06312},
      pages        = {281–298},
      year         = {2023},
      abstract     = {The interactions of amino acid side-chains confer diverse
                      energetic contributions and physical properties to a
                      protein’s stability and function. Various computational
                      tools estimate the effect of changing a given amino acid on
                      the protein’s stability based on parametrized (free)
                      energy functions. When parametrized for the prediction of
                      protein stability in water, such energy functions can lead
                      to suboptimal results for other solvents, such as ionic
                      liquids (IL), aqueous ionic liquids (aIL), or salt
                      solutions. However, to our knowledge, no comprehensive data
                      are available describing the energetic effects of aIL on
                      intramolecular protein interactions. Here, we present the
                      most comprehensive set of potential of mean force (PMF)
                      profiles of pairwise protein–residue interactions to date,
                      covering 50 relevant interactions in water, the two
                      biotechnologically relevant aIL [BMIM/Cl] and [BMIM/TfO],
                      and [Na/Cl]. These results are based on a cumulated
                      simulation time of >1 ms. aIL and salt ions can weaken, but
                      also strengthen, specific residue interactions by more than
                      3 kcal mol–1, depending on the residue pair,
                      residue–residue configuration, participating ions, and
                      concentration, necessitating considering such interactions
                      specifically. These changes originate from a complex
                      interplay of competitive or cooperative noncovalent
                      ion–residue interactions, changes in solvent structural
                      dynamics, or unspecific charge screening effects and occur
                      at the contact distance but also at larger,
                      solvent-separated distances. This data provide explanations
                      at the atomistic and energetic levels for complex IL effects
                      on protein stability and should help improve the prediction
                      accuracies of computational tools that estimate protein
                      stability based on (free) energy functions.},
      cin          = {IBG-4 / NIC / JSC / IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-4-20200403 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      Forschergruppe Gohlke $(hkf7_20200501)$},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      $G:(DE-Juel1)hkf7_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36520535},
      UT           = {WOS:000918748100001},
      doi          = {10.1021/acs.jcim.2c01123},
      url          = {https://juser.fz-juelich.de/record/916528},
}