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Related Concept Videos

Protein Families02:47

Protein Families

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 locations, protein...
Protein and Protein Structure02:15

Protein and Protein Structure

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 can...
Protein Organization01:24

Protein Organization

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.
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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 form...
Protein and Protein Structures02:15

Protein and Protein Structures

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 can...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...

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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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SVM-PB-Pred: SVM based protein block prediction method using sequence profiles and secondary structures.

V Suresh, S Parthasarathy1

  • 1Department of Bioinformatics, School of Life Sciences, Bharathidasan University, Tiruchirappalli 620 024, Tamil Nadu, India. bdupartha@gmail.com.

Protein and Peptide Letters
|July 17, 2013
PubMed
Summary
This summary is machine-generated.

We developed SVM-PB-Pred, a web server using support vector machines (SVM) to predict protein blocks from amino acid sequences. It achieves approximately 53% accuracy using sequence profiles and predicted secondary structures.

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Area of Science:

  • Bioinformatics
  • Computational Biology
  • Structural Bioinformatics

Background:

  • Protein structure prediction is crucial for understanding protein function.
  • Accurate prediction of protein blocks can aid in determining protein structure and function.
  • Existing methods for protein block prediction have limitations.

Purpose of the Study:

  • To develop a novel web server, SVM-PB-Pred, for predicting protein blocks.
  • To evaluate the performance of support vector machine (SVM) models using various input features and datasets.
  • To provide a freely accessible tool for predicting protein block letters from amino acid sequences.

Main Methods:

  • Developed a support vector machine (SVM) based web server, SVM-PB-Pred.
  • Utilized input features including sequence profiles (PSSM) and secondary structures (SS) from DSSP, NPS@, and GOR4.
  • Trained and tested SVM models on four datasets (RS90, DB433, LI1264, SP1577) using self-consistency, cross-validation, and independent tests.

Main Results:

  • Maximum prediction accuracy of ~70% was achieved in self-consistency tests using PSSM+SS(DSSP) features on LI1264 and SP1577 datasets.
  • Prediction accuracies decreased in independent case tests to ~53% for PSSM+SS(NPS@) and ~43% for PSSM+SS(GOR4).
  • The SVM-PB-Pred server demonstrated a prediction accuracy of ~53% using the SP1577 dataset and NPS@ predicted secondary structures.

Conclusions:

  • SVM-PB-Pred provides a valuable tool for predicting protein blocks from amino acid sequences.
  • The choice of input features and datasets significantly impacts prediction accuracy.
  • The developed web server offers a practical solution for researchers in structural bioinformatics and related fields.