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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).
For proteins, this means predicting the formation of protein structures such as alpha helices and beta strands, while for nucleic acids it means predicting the formation of nucleic acid structures like helixes and stem-loop structures through base pairing and base stacking interactions. Secondary structure prediction can refer to:
List of notable protein secondary structure prediction programs. Name Method description Type Link Initial release RaptorX-SS8
Structure- and sequence-based prediction of DNA-binding sites in DNA-binding proteins can be performed on several web servers listed below. DISIS predicts DNA binding sites directly from the amino acid sequence and hence is applicable for all known proteins.
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.
The three final output nodes deliver a score for each secondary structure element for the central position of the window. Using the secondary structure with the highest score, PSIPRED generates the protein prediction. [9] The Q3 value is the fraction of residues predicted correctly in the secondary structure states, namely helix, strand, and ...
Many secondary structure prediction methods rely on variations of dynamic programming and therefore are unable to efficiently identify pseudoknots. While the methods are similar, there are slight differences in the approaches to RNA and DNA structure prediction.
Predicting protein tertiary structure from only its amino sequence is a very challenging problem (see protein structure prediction), but using the simpler secondary structure definitions is more tractable. Early methods of secondary-structure prediction were restricted to predicting the three predominate states: helix, sheet, or random coil.