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

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.
Authors:
 [1] ;  [2] ;  [3] ; ORCiD logo [4]
  1. Peking Univ., Beijing (China). School of Physics, State Key Lab. of Nuclear Physics; Case Western Reserve Univ., Cleveland, OH (United States). Dept. of Nutrition
  2. Brookhaven National Lab. (BNL), Upton, NY (United States)
  3. Peking Univ., Beijing (China). School of Physics, State Key Lab. of Nuclear Physics
  4. Case Western Reserve Univ., Cleveland, OH (United States). Dept. of Nutrition
Publication Date:
Report Number(s):
BNL-113721-2017-JA
Journal ID: ISSN 1948-7185
Grant/Contract Number:
SC0012704; R01GM114056; AC02-98CH10886; P41RR012408; P41GM103473
Type:
Accepted Manuscript
Journal Name:
Journal of Physical Chemistry Letters
Additional Journal Information:
Journal Volume: 8; Journal Issue: 2; Journal ID: ISSN 1948-7185
Publisher:
American Chemical Society
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1351733

Song, Lingshuang, Yang, Lin, Meng, Jie, and Yang, Sichun. Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study. United States: N. p., Web. doi:10.1021/acs.jpclett.6b02673.
Song, Lingshuang, Yang, Lin, Meng, Jie, & Yang, Sichun. Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study. United States. doi:10.1021/acs.jpclett.6b02673.
Song, Lingshuang, Yang, Lin, Meng, Jie, and Yang, Sichun. 2016. "Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study". United States. doi:10.1021/acs.jpclett.6b02673. https://www.osti.gov/servlets/purl/1351733.
@article{osti_1351733,
title = {Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental–Computational Study},
author = {Song, Lingshuang and Yang, Lin and Meng, Jie and Yang, Sichun},
abstractNote = {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.},
doi = {10.1021/acs.jpclett.6b02673},
journal = {Journal of Physical Chemistry Letters},
number = 2,
volume = 8,
place = {United States},
year = {2016},
month = {12}
}