By Liliana López Kleine, Víctor Andrés Vera Ruiz (auth.), Miguel P. Rocha, Florentino Fernández Riverola, Hagit Shatkay, Juan Manuel Corchado (eds.)
The fields of Bioinformatics and Computational Biology were turning out to be progressively over the past few years boosted through an expanding desire for computational thoughts which could successfully deal with the large quantities of information produced by way of the hot experimental ideas in Biology. This demands new algorithms and ways from fields comparable to information Integration, records, information Mining, desktop studying, Optimization, laptop technology and synthetic Intelligence.
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Extra info for Advances in Bioinformatics: 4th International Workshop on Practical Applications of Computational Biology and Bioinformatics 2010 (IWPACBB 2010)
Predicting the Start of Protein α-Helices 35 One can identify four types of structures in a protein. The primary structure of a protein corresponds to the linear sequence of residues. The secondary structure is composed by subsets of residues arranged as α-helices and β-sheets, as seen in Figure 2. The tertiary structure results for the folding of α-helices or β-sheets. Fig. 2 Secondary structure conThe quaternary structure results from the formations of a protein: α-helices interaction of two or more polypeptide (left); β-sheet (right) chains.
5. 6. at the start of a α-helix; at the end of a α-helix; in the interior of a α-helix; at the start of a β-strand; at the end of a β-strand; in the interior of a β-helix. To do so, we identify the “special” point where the secondary structures start or end, and then add W residues before and after that point. Therefore the sequences are of size 2 × W + 1, where W ∈ [2, 3, 4, 5]. In the interior of a secondary structure we just pick sequences of 2 × W + 1 residues that do not overlap. do Predicting the Start of Protein α-Helices 37 end of secondary structures.
New Science Press Ltd. (2007) 25. : The importance of protein folding. com/horizon/proteinfolding/background/importance. html 26. : Prediction of secondary structure of proteins from their amino acid sequence. Advances in Enzymology and Related Areas of Molecular Biology 47, 45–148 (1978) 27. 5: Programs for Machine Learning. Morgan Kaufmann Publishers, San Mateo (1993) 28. pdf 29. : Reductive cleavage of disulﬁde bridges in ribonuclease. Science 125, 691–692 (1957) 30. : Modelling the structure and function of enzymes by machine learning.
Advances in Bioinformatics: 4th International Workshop on Practical Applications of Computational Biology and Bioinformatics 2010 (IWPACBB 2010) by Liliana López Kleine, Víctor Andrés Vera Ruiz (auth.), Miguel P. Rocha, Florentino Fernández Riverola, Hagit Shatkay, Juan Manuel Corchado (eds.)