Prediction of protein secondary structure based on physical theory. Histones.
Secondary structures of histones H1, H2A, H2B, H3, H4 and H5 have been calculated by the computer program ALB based on a molecular theory of protein secondary structure. The predicted secondary structures of all histones are predominantly alpha-helical. The calculated secondary structure of linker histones H1 and H5 is close to that previously obtained from two-dimensional NMR data. For each of the core histones (H2A, H2B, H3, H4) one long alpha-helix and several short ones have been predicted. These long helices can be identified with rods in the low-resolution electron density map.
Ptitsyn
O B
OB
Institute of Protein Research, Academy of Sciences of the USSR, Moscow.
Finkelstein
A V
AV
D003198:Computer Simulation; D006657:Histones; D011237:Predictive Value of Tests; D011487:Protein Conformation
D006657:Histones