Application of the one-dimensional Ising model to the secondary structures in globular proteins. Prediction of beta-regions.
An attempt has been made to predict the beta-regions in 16 globular proteins by applying the one-dimensional Ising model theory of Lifson & Roig (8). The parameters for the theory have been derived from the statistical data on globular proteins given by Chou & Fasman (5). Comparison of our results with the data available from the X-ray crystallographic studies indicates a prediction accuracy which is comparable to those of several other methods, especially in view of the limitations in our method for considering the other secondary structures. It is pointed out that not considering the long-range interactions in our and other methods based on short-range interactions would make these methods incomplete and incapable of being uniformly applicable to all proteins.
D000596:Amino Acids / Q000032:analysis; D008956:Models, Chemical; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D014961:X-Ray Diffraction
D000596:Amino Acids; D011506:Proteins