Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study

Song, Lingshuang; Yang, Lin; Meng, Jie; Yang, Sichun

doi:10.1021/acs.jpclett.6b02673

Title: Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study

Journal Article · Thu Dec 29 00:00:00 EST 2016 · Journal of Physical Chemistry Letters

DOI:https://doi.org/10.1021/acs.jpclett.6b02673· OSTI ID:1351733

Song, Lingshuang ^[1]; Yang, Lin ^[2]; Meng, Jie ^[3];

^[4]

Peking Univ., Beijing (China). School of Physics, State Key Lab. of Nuclear Physics; Case Western Reserve Univ., Cleveland, OH (United States). Dept. of Nutrition
Brookhaven National Lab. (BNL), Upton, NY (United States)
Peking Univ., Beijing (China). School of Physics, State Key Lab. of Nuclear Physics
Case Western Reserve Univ., Cleveland, OH (United States). Dept. of Nutrition

Here, 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 inter-leucine 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 leucineleucine interacting landscape, where two leucine molecules are aligned mostly in a parallel fashion, as opposed to anti-parallel, but also allows us to derive effective leucine-leucine interactions in solution. Collectively, this combined approach of employing experimental scattering and molecular simulation enables a quantitative characterization on effective inter-molecular interactions of hydrophobic amino acids, critical for protein function and dynamics such as protein folding.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0012704; R01GM114056; AC02-98CH10886; P41RR012408; P41GM103473

OSTI ID:: 1351733

Report Number(s):: BNL-113721-2017-JA

Journal Information:: Journal of Physical Chemistry Letters, Vol. 8, Issue 2; ISSN 1948-7185

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 4 works

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