Ontology highlight
ABSTRACT:
SUBMITTER: Song L
PROVIDER: S-EPMC5256481 | biostudies-literature | 2017 Jan
REPOSITORIES: biostudies-literature
The journal of physical chemistry letters 20170103 2
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<sup>-1</sup>. Atomistic molecular dynamics simulations were then performed and compared with the scattering data, achieving high consis ...[more]