Physical properties of chicken erythrocyte HMG-1, HMG-2 and HMG-E.
HMG-1, HMG-2 and HMG-E were purified from chicken erythrocyte chromatin without exposure to overt denaturing conditions and subjected to several types of physical measurement. The principal conclusions drawn from the measurements were: none of the proteins has a strong tendency to self-associate, although HMG-1 does weakly self-associate; the frictional properties of HMG-1 and HMG-E (and probably HMG-2) indicate that the proteins deviate significantly from compact, moderately hydrated spheres; and each of the proteins contains approximately 40% helix and little if any beta-pleated sheet.
D000818:Animals; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002645:Chickens; D002942:Circular Dichroism; D004912:Erythrocytes / Q000032:analysis*; D006609:High Mobility Group Proteins / Q000097:blood* / Q000302:isolation & purification; D008970:Molecular Weight; D011487:Protein Conformation
D006609:High Mobility Group Proteins