Electrophoretic mobilities and migrating analytes: Part 2: Hydration.

A molecular modeling package has been used to systematically hydrate a series of previously built peptides. The volume data derived have been used with the log-log form of the inverse square law and published electrophoretic mobilities to test for the most likely states of hydration. Starting with the bare peptides and increasing hydration, however, the strength of correlation diminishes, indicating that the average electromigrating peptide is not extensively hydrated.

Electrophoretic mobilities and migrating analytes: Part 1: Relationships.

The molecular radii (r) of a series of peptides have been determined by molecular modeling. With these data, it is shown that electrophoretic mobility (mu(ep)) is proportional to 1/r2, and that the dependence presented in textbooks (mu(ep) infinity 1/r) is wrong. Use of the approximately equivalent, mass-based Offord equation is discussed, and other relevant considerations are presented.

Molecular mapping in the CNS.

Since ancient times the operation of the brain has elicited more than usual interest. Data mining of the human genome is revealing that many CNS abnormalities have a genetic component. As yet this information can not be used directly to cure or ameliorate specific CNS disorders although this is regarded as having great potential for future therapies.