TY - JOUR
T1 - Evidence for microscopic, long-range hydration forces for a hydrophobic amino acid
AU - Pertsemlidis, Alexander
AU - Soper, Alan K.
AU - Sorenson, Jon M.
AU - Head-Gordon, Teresa
PY - 1999/1/19
Y1 - 1999/1/19
N2 - We have combined neutron solution scattering experiments with molecular dynamics simulation to isolate an excess experimental signal that is caused solely by N-acetyl-leucine-amide (NALA) correlations in aqueous solution. This excess signal contains information about how NALA molecule centers are correlated in water, and we show how these solute-solute correlations might be determined at dilute concentrations in the small angle region. We have tested qualitatively different pair distribution functions for NALA molecule centers - gas, cluster, and aqueous forms of g(c)(r)and have found that the excess experimental signal is adequate enough to rule out gas and cluster pair distribution functions. The aqueous form of g(c)(r) that exhibits a solvent-separated minimum, and possibly longer-ranged correlations as well, is not only physically sound but reproduces the experimental data reasonably well. This work demonstrates that important information in the small angle region can be mined to resolve solute-solute correlations, their lengthscales, and thermodynamic consequences even at dilute concentrations. The hydration forces that operate on the microscopic scale of individual amino acid side chains, implied by the small angle scattering data, could have significant effects on the early stages of protein folding, on ligand binding, and on other intermolecular interactions.
AB - We have combined neutron solution scattering experiments with molecular dynamics simulation to isolate an excess experimental signal that is caused solely by N-acetyl-leucine-amide (NALA) correlations in aqueous solution. This excess signal contains information about how NALA molecule centers are correlated in water, and we show how these solute-solute correlations might be determined at dilute concentrations in the small angle region. We have tested qualitatively different pair distribution functions for NALA molecule centers - gas, cluster, and aqueous forms of g(c)(r)and have found that the excess experimental signal is adequate enough to rule out gas and cluster pair distribution functions. The aqueous form of g(c)(r) that exhibits a solvent-separated minimum, and possibly longer-ranged correlations as well, is not only physically sound but reproduces the experimental data reasonably well. This work demonstrates that important information in the small angle region can be mined to resolve solute-solute correlations, their lengthscales, and thermodynamic consequences even at dilute concentrations. The hydration forces that operate on the microscopic scale of individual amino acid side chains, implied by the small angle scattering data, could have significant effects on the early stages of protein folding, on ligand binding, and on other intermolecular interactions.
KW - Hydration structure
KW - Protein folding
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U2 - 10.1073/pnas.96.2.481
DO - 10.1073/pnas.96.2.481
M3 - Article
C2 - 9892659
AN - SCOPUS:0033582271
SN - 0027-8424
VL - 96
SP - 481
EP - 486
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 2
ER -