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Predicts secondary structure and solvent accessibility: Webserver: server and API: 1998 PredictProtein: Profile-based neural network: Webserver: server: 1992 PSIPRED: two feed-forward neural networks which perform an analysis on output obtained from PSI-BLAST: Webserver: server: 1999
PSI-blast based secondary structure PREDiction (PSIPRED) is a method used to investigate protein structure. It uses artificial neural network machine learning methods in its algorithm. [ 2 ] [ 3 ] [ 4 ] It is a server-side program, featuring a website serving as a front-end interface, which can predict a protein's secondary structure ( beta ...
Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.
Jpred v.4 is the latest version of the JPred Protein Secondary Structure Prediction Server [1] which provides predictions by the JNet algorithm, one of the most accurate methods for secondary structure prediction, [2] that has existed since 1998 in different versions.
Secondary structure prediction is a set of techniques in bioinformatics that aim to predict the secondary structures of proteins and nucleic acid sequences based only on knowledge of their primary structure.
An email is sent to the user together with a link to a web page of results. RaptorX Server currently generates the following results: 3-state and 8-state secondary structure prediction, sequence-template alignment, 3D structure prediction, solvent accessibility prediction, disorder prediction and binding site prediction.
Structure prediction methods: secondary structure, solvent accessibility and membrane helices predicted by the PHD and PROF programs, [7] [8] membrane strands predicted by PROFtmb, [9] coiled-coil regions by COILS, [10] and inter-residue contacts through PROFcon, [11] low-complexity regions are marked by SEG [12] and long regions with no ...
Secondary structure-related Method that uses the distribution of hydrophobic and electrostatic patches on the surface of the protein, factoring in the intensity and relative orientation of the respective surface patches into an aggregation propensity function that has been trained on a benchmark set of 31 adnectin proteins.