Abstract

The prediction of the secondary structure of a protein from its amino acid sequence is an important step towards the prediction of its three-dimensional structure. While many of the existing algorithms utilize the similarity and homology to proteins with known secondary structures in the Protein Data Bank, other proteins with low similarity measures require a single sequence approach to the discovery of their secondary structure. In this paper we propose an algorithm based on the deterministic sequential sampling method and hidden Markov model for the single-sequence protein secondary structure prediction. The predictions are made based on windowed observations and by the weighted average over possible conformations within the observation window. The proposed algorithm is shown to achieve better performance on real dataset compared to the existing single-sequence algorithm.

Highlights

  • In living organisms, numerous proteins are utilized to carry out important cellular functions

  • The zinc fingers are one such family of proteins that often act as transcription factors, which recognize specific patterns of DNA sequences through the different amino acids found on the finger-like structure [2]

  • The real dataset we used in our experiment is a set of proteins with low sequence homology chosen from the Protein Data Bank (PDB)

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Summary

Introduction

Numerous proteins are utilized to carry out important cellular functions. When processing the current amino acid, instead of terminating the latest segment at the current position, we will enumerate all possible conformations within the given window, and take a weighted average to determine the most likely secondary structure assignment.

Results
Conclusion
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