| Literature DB >> 35502337 |
Arshpreet Kaur1, Abhijit Chitre2, Kirti Wanjale3, Pankaj Kumar4, Shahajan Miah5, Arnold C Alguno6.
Abstract
Protein is the material foundation of living things, and it directly takes part in and runs the process of living things itself. Predicting protein complexes helps us understand the structure and function of complexes, and it is an important foundation for studying how cells work. Genome-wide protein interaction (PPI) data is growing as high-throughput experiments become more common. The aim of this research is that it provides a dual-tree complex wavelet transform which is used to find out about the structure of proteins. It also identifies the secondary structure of protein network. Many computer-based methods for predicting protein complexes have also been developed in the field. Identifying the secondary structure of a protein is very important when you are studying protein characteristics and properties. This is how the protein sequence is added to the distance matrix. The scope of this research is that it can confidently predict certain protein complexes rapidly, which compensates for shortcomings in biological research. The three-dimensional coordinates of C atom are used to do this. According to the texture information in the distance matrix, the matrix is broken down into four levels by the double-tree complex wavelet transform because it has four levels. The subband energy and standard deviation in different directions are taken, and then, the two-dimensional feature vector is used to show the secondary structure features of the protein in a way that is easy to understand. Then, the KNN and SVM classifiers are used to classify the features that were found. Experiments show that a new feature called a dual-tree complex wavelet can improve the texture granularity and directionality of the traditional feature extraction method, which is called secondary structure.Entities:
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Year: 2022 PMID: 35502337 PMCID: PMC9056223 DOI: 10.1155/2022/2273648
Source DB: PubMed Journal: Biomed Res Int Impact factor: 3.246
Figure 1RNA polymerase.
Figure 2Protein-protein interaction network.
Dataset.
| Dataset |
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| Total |
|---|---|---|---|---|---|
| A | 48 | 60 | 45 | 44 | 197 |
| B | 440 | 437 | 342 | 437 | 1656 |
Figure 3Texture map of different protein secondary structures.
Figure 4Decomposition of two-dimensional DT-CWT.
Performance prediction of proposed work over dataset A.
| Parameter | Proposed structure | |||
|---|---|---|---|---|
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| Sensitivity | 92.56 | 94.26 | 90.56 | 92.23 |
| Specificity | 95.56 | 96.28 | 93.45 | 94.12 |
| Accuracy | 96.45 | 98.56 | 94.62 | 95.68 |
| MCC | 94.24 | 96.45 | 92.12 | 93.58 |
Performance prediction of proposed work over dataset B.
| Parameter | Proposed structure | |||
|---|---|---|---|---|
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| Sensitivity | 95.45 | 93.41 | 89.45 | 93.41 |
| Specificity | 96.45 | 95.26 | 89.25 | 95.23 |
| Accuracy | 98.12 | 98.45 | 92.85 | 96.48 |
| MCC | 97.12 | 95.12 | 91.57 | 95.12 |
Comparative performance prediction over dataset A.
| Extract features | Proposed structure | ||||
|---|---|---|---|---|---|
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| OA | |
| Grayscale histogram | 78.56 | 79.23 | 75.23 | 85.68 | 86.78 |
| Grey-level cooccurrence matrix | 76.23 | 76.48 | 74.24 | 79.48 | 82.56 |
| Wavelet energy | 79.23 | 80.45 | 75.28 | 82.45 | 84.89 |
| Double-tree complex wavelet | 80.12 | 82.23 | 79.46 | 85.56 | 89.46 |
Comparative performance prediction over dataset B.
| Extract features |
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| OA |
|---|---|---|---|---|---|
| Grayscale histogram | 79.56 | 81.28 | 76.25 | 87.26 | 89.52 |
| Grey-level cooccurrence matrix | 77.42 | 77.98 | 75.68 | 89.26 | 92.12 |
| Wavelet energy | 80.56 | 82.4 | 78.26 | 84.56 | 88.45 |
| Double-tree complex wavelet | 81.89 | 83.47 | 80.45 | 89.26 | 90.12 |
Figure 5Performance prediction of proposed work over dataset A.
Figure 6Performance prediction of proposed work over dataset B.
Figure 7Comparative performance prediction over dataset A.
Figure 8Comparative performance prediction over dataset B.