Abstract
The rapidly growing structure databases enhance the probability of finding identical sequences sharing structural similarity. Structure prediction methods are being used extensively to abridge the gap between known protein sequences and the solved structures which is essential to understand its specific biochemical and cellular functions. In this work, we plan to study the ambiguity between sequence-structure relationships and examine if sequentially identical peptide fragments adopt similar three-dimensional structures. Fragments of varying lengths (five to ten residues) were used to observe the behavior of sequence and its three-dimensional structures. The STAMP program was used to superpose the three-dimensional structures and the two parameters (Sequence Structure Similarity Score (Sc) and Root Mean Square Deviation value) were employed to classify them into three categories: similar, intermediate and dissimilar structures. Furthermore, the same approach was carried out on all the three-dimensional protein structures solved in the two organisms, Mycobacterium tuberculosis and Plasmodium falciparum to validate our results.
Keywords: Identical peptides, non-redundant structures, protein data bank, protein fragments, structural similarity, Plasmodium falciparum, Mycobacterium tuberculosis, fragments, organisms, parameters
Current Bioinformatics
Title:Sequence-Structure Similarity: Do Sequentially Identical Peptide Fragments have Similar Three-Dimensional Structures?
Volume: 7 Issue: 2
Author(s): Muthukumarasamy Uthayakumar, Sanjeev Patra, Raju Nagarajan and Kanagaraj Sekar
Affiliation:
Keywords: Identical peptides, non-redundant structures, protein data bank, protein fragments, structural similarity, Plasmodium falciparum, Mycobacterium tuberculosis, fragments, organisms, parameters
Abstract: The rapidly growing structure databases enhance the probability of finding identical sequences sharing structural similarity. Structure prediction methods are being used extensively to abridge the gap between known protein sequences and the solved structures which is essential to understand its specific biochemical and cellular functions. In this work, we plan to study the ambiguity between sequence-structure relationships and examine if sequentially identical peptide fragments adopt similar three-dimensional structures. Fragments of varying lengths (five to ten residues) were used to observe the behavior of sequence and its three-dimensional structures. The STAMP program was used to superpose the three-dimensional structures and the two parameters (Sequence Structure Similarity Score (Sc) and Root Mean Square Deviation value) were employed to classify them into three categories: similar, intermediate and dissimilar structures. Furthermore, the same approach was carried out on all the three-dimensional protein structures solved in the two organisms, Mycobacterium tuberculosis and Plasmodium falciparum to validate our results.
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Cite this article as:
Uthayakumar Muthukumarasamy, Patra Sanjeev, Nagarajan Raju and Sekar Kanagaraj, Sequence-Structure Similarity: Do Sequentially Identical Peptide Fragments have Similar Three-Dimensional Structures?, Current Bioinformatics 2012; 7(2) . https://dx.doi.org/10.2174/157489312800604345
DOI https://dx.doi.org/10.2174/157489312800604345 |
Print ISSN 1574-8936 |
Publisher Name Bentham Science Publisher |
Online ISSN 2212-392X |

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