Comparison between histones FV and F2a2 of chicken erythrocyte. I. Structure, stability and conformation of the free proteins.
Purified chicken erythrocyte histones FV and F2a2 were studied by means of circular dichroism as a function of ionic strength and temperature. The percentage of alpha-helical regions was calculated by comparison with reference spectra obtained with four standard proteins of known tertiary structure. Maximal alpha-helical organization, reached in high ionic strength, was estimated to 14% and 23% for FV and F2a2 respectively. We have compared our experimental determinations of the secondary structure of F2a2 with predictions made from amino-acid sequence according to Fasman's rules. When instability induced by the presence of charged residues close together is taken into account, a good agreement is found between predicted and observed values. The thermal denaturation of FV is cooperative and, unlike F2a2, seems to obey a two-state transition. The classical Arrhenius plot is linear, which indicates that the heat capacity is the same in both the native and the denatured state. Such a behaviour is typical of an expanded configuration of FV even in the "native" state.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D002942:Circular Dichroism; D004355:Drug Stability; D004912:Erythrocytes / Q000032:analysis*; D006657:Histones / Q000097:blood; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D000596:Amino Acids; D006657:Histones