We present a joint experimental–computational
study to quantitatively
describe the thermodynamics of hydrophobic leucine amino acids in
aqueous solution. X-ray scattering data were acquired at a series
of solute and salt concentrations to effectively measure interleucine
interactions, indicating that a major scattering peak is observed
consistently at q = 0.83 Å–1. Atomistic molecular dynamics simulations were then performed and
compared with the scattering data, achieving high consistency at both
small and wider scattering angles (q = 0–1.5
Å–1). This experimental–computational
consistence enables a first glimpse of the leucine–leucine
interacting landscape, where two leucine molecules are aligned mostly
in a parallel fashion, as opposed to antiparallel, but also allows
us to derive effective leucine–leucine interactions in solution.
Collectively, this combined approach of employing experimental scattering
and molecular simulation enables quantitative characterization of
effective intermolecular interactions of hydrophobic amino acids,
critical for protein function and dynamics such as protein folding.
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