Related Experiment Video
Updated: Jun 17, 2026
06:50
Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
PreDisorder: ab initio sequence-based prediction of protein disordered regions
Xin Deng1, Jesse Eickholt, Jianlin Cheng
1Department of Computer Science, University of Missouri-Columbia, Columbia, MO 65211, USA. xd9d3@mail.missouri.edu
BMC Bioinformatics
|December 23, 2009
Summary
PreDisorder is a new server for predicting protein disordered regions. It uses an ab initio method and performs comparably to top predictors, enabling genomic-scale analysis.
Area of Science:
- Biochemistry and Molecular Biology
- Bioinformatics and Computational Biology
Background:
- Protein disordered regions lack stable structures but are crucial for protein expression and function.
- Accurate prediction of these regions is vital for protein structure prediction, determination, and function annotation.
Purpose of the Study:
- To introduce PreDisorder, a novel computational server for predicting protein disordered regions.
- To evaluate the performance of PreDisorder against existing protein disorder prediction methods.
Main Methods:
- The PreDisorder server is based on the MULTICOM-CMFR ab initio prediction method.
- Performance was benchmarked against 26 other predictors using the CASP8 dataset and various accuracy measures.
Main Results:
- PreDisorder demonstrated favorable performance compared to other ab initio methods.
- Its accuracy was found to be comparable to leading meta and clustering prediction methods.
Conclusions:
- PreDisorder offers a fast and reliable solution for predicting protein disordered regions at a genomic scale.
- The server is accessible online for researchers to utilize.
Related Concept Videos
02:18Intrinsically Disordered Proteins
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
02:18Intrinsically Disordered Proteins
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
02:26Conservation 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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
01:24Protein 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.
The primary structure of a protein is its amino acid sequence.
02:26Conservation of Protein Domains
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...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...