Advancing remote homology detection: A step toward understanding and accurately predicting protein function
1Khoury College of Computer Sciences, Northeastern University, Boston, MA 02115, USA.
Cell Systems
|June 16, 2022
Summary
A new deep-learning method significantly expands the Protein Family (Pfam) database, identifying 6.8 million new protein members. This breakthrough accelerates the understanding of protein evolution, structure, and function.
Area of Science:
- Bioinformatics
- Computational Biology
- Molecular Evolution
Background:
- Homologous proteins with divergent sequences are crucial for understanding protein evolution, structure, and function.
- Traditional methods for identifying protein families have a limited discovery rate.
Purpose of the Study:
- To develop a novel deep-network-based method for identifying homologous proteins.
- To significantly increase the number of known protein family members in the Pfam database.
Main Methods:
- Utilized a deep-learning network architecture.
- Applied the method to identify new members within protein families.
- Compared the discovery rate with traditional approaches.
Main Results:
- Identified 6.8 million new protein family members, a substantial increase.
- The deep-network method achieved a higher discovery rate than traditional approaches over a decade.
- Demonstrated the efficacy of deep learning in protein family identification.
Conclusions:
- Deep learning offers a powerful approach for expanding protein family databases.
- The newly identified members provide valuable data for studying protein evolution, structure, and function.
- This method represents a significant advancement in bioinformatics for protein family analysis.
Related Concept Videos
Protein Families
15.7K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...
15.7K
Conservation of Protein Domains Over Different Proteins
11.3K
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...
11.3K
Conserved Binding Sites
4.3K
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...
4.3K
Protein Networks
4.1K
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,...
4.1K
Conservation of Protein Domains
3.2K
3.2K
Protein-protein Interfaces
13.2K
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...
13.2K


