Model of protein conformation in the reversed-phase separation of interleukin-2 muteins.
Thirty muteins* of interleukin-2 were studied by reversed-phase high-performance liquid chromatography in a gradient mode. Values of the stoichiometry-factor Z [from Geng and Regnier, J. Chromatogr., 296 (1984) 15] varied over a 2.5-fold range for these proteins of similar molecular weight and composition. It is proposed that the more hydrophobic and/or more stable proteins have smaller values of Z while the larger Z-values correspond to a higher degree of protein unfolding during reversed-phase retention. The practical utility of this approach was demonstrated when these Z values were used to predict correctly a reversal in elution order for two closely related interleukin-2 muteins, when shallower gradients were used.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007376:Interleukin-2 / Q000302:isolation & purification*; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000302:isolation & purification
D000596:Amino Acids; D007376:Interleukin-2; D011994:Recombinant Proteins