一个CNN-CBAM-BIGRU模型用于蛋白质功能预测
Lavkush Sharma1, Akshay Deepak1, Ashish Ranjan2
1Department of Computer Science and Engineering, 230635 National Institute of Technology Patna , Patna, Bihar, India.
概括
一个新的深度学习模型,CNN-CBAM+BiGRU,通过整合注意力机制和循环神经网络来增强蛋白质功能预测. 这种方法提高了识别细胞组件,分子功能和生物过程的准确性.
科学领域:
- 生物信息学是一种生物信息学.
- 计算生物学 计算生物学
- 机器学习 机器学习
背景情况:
- 从氨基酸序列预测蛋白质功能是生物信息学的一个基本挑战.
- 深度学习模型在自动化特征提取以预测蛋白质功能方面表现出有希望.
- 现有的方法往往难以捕捉复杂的序列依赖性.
研究的目的:
- 提出一种新的深度学习模型,CNN-CBAM+BiGRU,用于改进蛋白质功能预测.
- 为了利用注意力机制,从蛋白质序列中更有效地提取特征.
- 为了增强蛋白质序列中长距离依赖的捕获.
主要方法:
- 这项研究引入了一种混合模型,将卷积神经网络 (CNN) 与卷积块注意模块 (CBAM) 和双向门循环单元 (BiGRU) 结合起来.
- CBAM指导CNN专注于蛋白质序列的突出区域,改善特征表示.
- 双GRU被用来有效地建模功能预测至关重要的远程顺序依赖关系.
主要成果:
- 与CNN-BIGRU+ATT模型相比,CNN-CBAM+BiGRU模型在人类和酵母数据集上的表现优越.
- 对于人类数据集,观察到 +1.0% (细胞组件), +1.1% (分子功能) 和 +0.5% (生物过程) 的改善.
- 对于酵母数据集,该模型实现了更高的准确性,获得了 +2.4% (细胞组成部分), +1.2% (分子功能) 和 +0.6% (生物过程).
结论:
- 整合CBAM和BiGRU显著提高了蛋白质功能预测的准确性.
- 拟议的模型提供了一种更有效的方法,用于特征提取和蛋白质序列中的依赖性建模.
- 这一进步有可能通过更精确的蛋白质功能注释来加速生物研究.
相关概念视频
Protein Organization
6.4K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.4K
Conservation of Protein Domains Over Different Proteins
10.8K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.8K
Protein and Protein Structure
79.4K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.4K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Protein Networks
3.9K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
3.9K
Protein-protein Interfaces
12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K


