iSuc-PseAAC: predicting lysine succinylation in proteins by incorporating peptide position-specific propensity
Yan Xu1, Ya-Xin Ding1, Jun Ding1
1Department of Information and Computer Science, University of Science and Technology Beijing, Beijing 100083, China.
Scientific Reports
|June 19, 2015
Summary
A new computational method, iSuc-PseAAC, predicts lysine succinylation sites on proteins. This post-translational modification predictor achieves high accuracy and offers a user-friendly web server for researchers.
Area of Science:
- Biochemistry
- Proteomics
- Bioinformatics
Background:
- Lysine succinylation is a crucial post-translational modification (PTM) of proteins.
- Succinylation is implicated in various disease states.
- Experimental identification of succinylated sites is recent, necessitating computational approaches.
Purpose of the Study:
- To develop an accurate computational method for identifying protein lysine succinylation sites.
- To create a user-friendly web server for predicting succinylation sites.
Main Methods:
- Incorporation of peptide position-specific propensity into pseudo amino acid composition.
- Development of the iSuc-PseAAC predictor.
- Utilizing a support vector machine algorithm with rigorous leave-one-out cross-validation on a benchmark dataset.
Main Results:
- The iSuc-PseAAC predictor achieved 79.94% accuracy, 51.07% sensitivity, 89.42% specificity, and a MCC of 0.431.
- The predictor demonstrated promising performance on a stringent benchmark dataset.
- A user-friendly web server is available for public use.
Conclusions:
- The iSuc-PseAAC predictor is a promising computational tool for identifying protein lysine succinylation sites.
- This method can serve as a valuable high-throughput tool in PTM research.
- The accessible web server facilitates research without requiring deep mathematical understanding.
More Related Videos
Related Concept Videos
Conserved Binding Sites
5.3K
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...
5.3K
Covalently Linked Protein Regulators
9.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
9.9K
Ligand Binding Sites
15.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.8K
Amino acids
111.2K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
111.2K


