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The Prediction of the Secondary Structure of Proteins
1991The prediction of the secondary structure of proteins has been widely applied to many areas of protein chemistry. This review gives an overview of its utility, reliability and application to a wide variety of problems in the life sciences.
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Secondary structure prediction and protein design.
Biochemical Society symposium, 1990For non-homologous proteins, and after cross-validation, the methods reviewed in this article exhibit a probability index (percentage of correctly predicted residues per predicted residues) of 59-65.5% according to the methods employed with a standard deviation of 7% for three conformational states: alpha-helix, beta-strand and coil.
Garnier, Jean +3 more
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Redefining the goals of protein secondary structure prediction
Journal of Molecular Biology, 1994Secondary structure prediction recently has surpassed the 70% level of average accuracy, evaluated on the single residue states helix, strand and loop (Q3). But the ultimate goal is reliable prediction of tertiary (three-dimensional, 3D) structure, not 100% single residue accuracy for secondary structure.
Burkhard Rost +2 more
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PHD - an automatic mail server for protein secondary structure prediction
Comput. Appl. Biosci., 1994By the middle of 1993, > 30,000 protein sequences has been listed. For 1000 of these, the three-dimensional (tertiary) structure has been experimentally solved. Another 7000 can be modelled by homology.
B. Rost, C. Sander, R. Schneider
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Secondary structure prediction and determination of proteins — a review
International Journal of Peptide and Protein Research, 1988The rapid increase in sequence data in combination with a greater understanding of the forces regulating protein structure has been the impetus for an upsurge in the development of theoretical prediction methods. These methods have afforded protein chemists the ability to identify and quantify the various secondary structures along the protein chain ...
Shuryo Nakai +2 more
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Reaching optimized parameter set: protein secondary structure prediction using neural network
Neural computing & applications (Print), 2016We propose an optimized parameter set for protein secondary structure prediction using three-layer feed forward back propagation neural network. The methodology uses four parameters viz. encoding scheme, window size, number of neurons in the hidden layer
Jyotshna Dongardive, Siby Abraham
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Prediction of protein secondary structures by a neural network
Bioinformatics, 1993We have studied the prediction of globular protein secondary structures by neural networks. Protein secondary structures are allocated to amino acid residues using Kabsch and Sander's dictionary of protein secondary structures and the neural network is taught the protein secondary structures.
Koji Tajima, Fumiyoshi Sasagawa
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Accurate Prediction of Protein Secondary Structural Content
Journal of Protein Chemistry, 2001An improved multiple linear regression (MLR) method is proposed to predict a protein's secondary structural content based on its primary sequence. The amino acid composition, the autocorrelation function, and the interaction function of side-chain mass derived from the primary sequence are taken into account.
Xian-Ming Pan, Zong Lin
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Hybrid system for protein secondary structure prediction
Journal of Molecular Biology, 1992We have developed a hybrid system to predict the secondary structures (alpha-helix, beta-sheet and coil) of proteins and achieved 66.4% accuracy, with correlation coefficients of C(coil) = 0.429, C alpha = 0.470 and C beta = 0.387. This system contains three subsystems ("experts"): a neural network module, a statistical module and a memory-based ...
Xiru Zhang +2 more
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Secondary structure prediction of seed storage proteins
International Journal of Peptide and Protein Research, 1983The comparison of partial primary structure of seed storage proteins leads to show homologies inside of each considered family (Legume seed legumins and cereal prolamins). Predicted secondary structures deduced from the presently known sequences also exhibit considerable homologies, which implies a severe conservatism of these proteins.
Jean-Claude Pernollet, J. Mossé
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