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. The shapes of the peptides are predominantly oblate ellipsoidal, but generally do not deviate significantly from spherical and progressive hydration increases this trend. Thus, shape correction does not play a significant role in the calculations.
Cross
Reginald F
RF
School of Engineering and Science, Environment & Biotechnology Centre, Swinburne University of Technology, Hawthorn, Victoria, Australia. rcross@swin.edu.au
Wong
Margaret G
MG
D000595:Amino Acid Sequence; D000596:Amino Acids; D019075:Electrophoresis, Capillary / Q000379:methods*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification*; D014867:Water
D000596:Amino Acids; D009842:Oligopeptides; D010455:Peptides; D014867:Water