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Online Journal of Bioinformatics©
Volume 20(1):23-31, 2019.
Prediction patterns for initiation region of a- helix of proteins.
Baby Joseph1 and Vrundha M. Nair2
1Department(s) of Biotechnology, 2Bioinformatics, Malankara Catholic College, Mariagiri, Kaliakkavilai - 629153, Kanyakumari District, TamilNadu, India.
Joseph B, Nair VM., Prediction patterns for initiation region of a- helix of proteins, Onl J Bioinform., 20(1):23-31, 2019. The role of secondary and tertiary structure in protein folding remains unknown. Experiments show that not all the proteins fold spontaneously in the cell. Molecular chaperon proteins assist target proteins to initiate folding paths. Elucidation of protein folding may assist treatment of Alzheimer’s, Huntington’s, Parkinson's, CJD, Mad Cow (BSE), and cancer. Prediction of conserved patterns of secondary structural elements could increase accuracy of secondary structure prediction and protein folding. We describe conserved patterns in the initiation region of the alpha helix. The 3D structural details of PDB flat files and PERL were used to identify frequency of triplet occurrence in upstream and downstream initiation site of alpha helix. Three high propensity conserved patterns were identified in the initiation region of the alpha helix.
Keywords: alpha helix, protein folding, initiation site, PERL, PDB.