Differences in hydration structure near hydrophobic and hydrophilic amino acids.
AUTOR(ES)
Head-Gordon, T
RESUMO
We use molecular dynamics to simulate recent neutron scattering experiments on aqueous solutions of N-acetyl-leucine-amide and N-acetyl-glutamine-amide, and break down the total scattering function into contributions from solute-solute, solute-water, water-water, and intramolecular correlations. We show that the shift of the main diffraction peak to smaller angle that is observed for leucine, but not for glutamine, is attributable primarily to alterations in water-water correlations relative to bulk. The perturbation of the water hydrogen-bonded network extends roughly two solvation layers from the hydrophobic side chain surface, and is characterized by a distribution of hydrogen bonded ring sizes that are more planar and are dominated by pentagons in particular than those near the hydrophilic side chain. The different structural organization of water near the hydrophobic solute that gives rise to the inward shift in the main neutron diffraction peak under ambient conditions may also provide insight into the same directional shift for pure liquid water as it is cooled and supercooled.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1181111Documentos Relacionados
- 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.
- Biochemical and immunological differences between hydrophobic and hydrophilic strains of Streptococcus mutans.
- Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid.
- The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids.
- Thermal perturbation differential spectra of ribonucleic acids. I. Hydration effects.