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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 ...
List of notable protein secondary structure prediction programs. Name ... server download: ... server: 1992 PSIPRED:
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.
BAR 3.0 is a server for the annotation of protein sequences relying on a comparative large-scale analysis on the entire UniProt. With BAR 3.0 and a sequence you can annotate when possible: function (Gene Ontology), structure (Protein Data Bank), protein domains (Pfam).
PredictProtein (PP) is an automatic service that searches up-to-date public sequence databases, creates alignments, and predicts aspects of protein structure and function. Users send a protein sequence and receive a single file with results from database comparisons and prediction methods.
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
HHpred servers have been ranked among the best servers during CASP7, 8, and 9, for blind protein structure prediction experiments. In CASP9, HHpredA, B, and C were ranked 1st, 2nd, and 3rd out of 81 participating automatic structure prediction servers in template-based modeling [ 11 ] and 6th, 7th, 8th on all 147 targets, while being much ...
Secondary structure-related. Predict the probability that particular portions of a protein will form amyloid. sequence length Amyloidogenic regions FoldAmyloid [17] 2010 Web Server - FoldAmyloid: Secondary structure-related. Prediction of amyloid regions using expected probability of hydrogen bonds formation and packing densitites of residues ...