Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid.

AUTOR(ES)

Pertsemlidis, A

RESUMO

Neutron scattering experiments are used to determine scattering profiles for aqueous solutions of hydrophobic and hydrophilic amino acid analogs. Solutions of hydrophobic solutes show a shift in the main diffraction peak to smaller angle as compared with pure water, whereas solutions of hydrophilic solutes do not. The same difference for solutions of hydrophobic and hydrophilic side chains is also predicted by molecular dynamics simulations. The neutron scattering curves of aqueous solutions of hydrophobic amino acids at room temperature are qualitatively similar to differences between the liquid molecular structure functions measured for ambient and supercooled water. The nonpolar solute-induced expansion of water structure reported here is also complementary to recent neutron experiments where compression of aqueous solvent structure has been observed at high salt concentration.

Documentos Relacionados

• Evidence for microscopic, long-range hydration forces for a hydrophobic amino acid
• Differences in hydration structure near hydrophobic and hydrophilic amino acids.
• A Hydrophobic Segment within the 81-Amino-Acid Domain of TFIIIA from Saccharomyces cerevisiae Is Essential for Its Transcription Factor Activity
• Structure and dynamics of primary hydration shell of phosphatidylcholine bilayers at subzero temperatures.
• Structure of Caulobacter deoxyribonucleic acid.