A novel approach to prediction of the 3‐dimensional structures of protein backbones by neural networks
- 12 February 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 261 (1), 43-46
- https://doi.org/10.1016/0014-5793(90)80632-s
Abstract
Three-dimensional structures of protein backbones have been predicted using neural networks. A feed forward neural network was trained on a class of functionally, but not structurally, homologous proteins, using backpropagation learning. The network generated tertiary structure information in the form of binary distance constraints for the Cα atoms in the protein backbone. The binary distance between two Cα atoms was 0 if the distance between them was less than a certain threshold distance, and 1 otherwise. The distance constraints predicted by the trained neural network were utilized to generate a folded conformation of the protein backbone, using a steepest descent minimization approach.This publication has 22 references indexed in Scilit:
- Determination of the complete three-dimensional structure of the α-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometryJournal of Molecular Biology, 1988
- Predicting the secondary structure of globular proteins using neural network modelsJournal of Molecular Biology, 1988
- Prediction of probable pathways of folding in globular proteinsJournal of Protein Chemistry, 1988
- Prediction of the packing arrangement of strands in β-sheets of globular proteinsJournal of Protein Chemistry, 1988
- Prediction of the location of structural domains in globular proteinsJournal of Protein Chemistry, 1988
- Protein folding by restrained energy minimization and molecular dynamicsJournal of Molecular Biology, 1983
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- Algorithms for prediction of α-helical and β-structural regions in globular proteinsJournal of Molecular Biology, 1974
- Recognition of structural domains in globular proteinsJournal of Molecular Biology, 1974