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Two independent approaches were used to determine the three-dimensional solution structure of the trisaccharide fragment Lewis x determinant. The first approach utilized high-resolution nuclear magnetic resonance spectroscopy while the second consisted of conformational energy calculations and molecular dynamnics simulations. Both approaches yielded the same average rigid structure for the Lewis x trisaccharide.

The effects of urea on protein stability are studied by using all-atom molecular dynamics simulations of ubiquitin, G311 protein, and immunoglobulin binding domain (B1) of streptococcal protein G (GB1) in water and 8 M aqueous urea solution. Urea has replaced the protein-protein and protein-water contacts by forming stronger contacts with the protein, which is shown by the longer survival times of the protein-urea hydrogen bonds.

The hydrodynamic properties of enkephalins in the presence of a potential intermediate receptor, ganglioside GM1, are investigated and the components that take a major role in the peptide-lipid binding are identified. The results indicate that the direct interaction between neuropeptide enkephalins and ganglioside GM1 are mainly through the central two residues of the peptides indicating a hydrophobic interaction.