Related Experiment Video
Updated: May 26, 2026
07:08
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Coevolved residues and the functional association for intrinsically disordered proteins
1Department of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology (KAIST), Yuseong-gu, Daejeon, Republic of Korea.
Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
|December 17, 2011
Summary
Coevolution analysis reveals fewer associations between disordered residues in intrinsically disordered proteins. This finding aids in predicting protein disorder and understanding their biological functions from sequence data.
Area of Science:
- * Evolutionary biology
- * Molecular biology
- * Bioinformatics
Background:
- * Intrinsically disordered proteins (IDPs) lack stable 3D structures.
- * Evolutionary studies of IDPs typically focus on individual residue changes (substitutions, conservation).
- * The evolutionary relationships *between* disordered residues remain underexplored.
Purpose of the Study:
- * To investigate the patterns of residue-residue coevolution within disordered protein regions.
- * To determine if coevolutionary signals differ between disordered and ordered protein segments.
- * To explore the utility of coevolution information for predicting protein disorder and function.
Main Methods:
- * Analysis of residue-residue coevolutionary patterns in disordered protein sequences.
- * Comparison of coevolutionary metrics in disordered versus ordered regions.
- * Examination of coevolution and conservation distributions across different functional categories of disordered proteins.
Main Results:
- * Coevolved residue interactions are significantly reduced in disordered regions, irrespective of sequence propensity.
- * The distribution patterns of coevolved and conserved residues are distinct and vary by functional category.
- * Coevolutionary information provides insights into the unique evolutionary pressures on disordered regions.
Conclusions:
- * Coevolutionary analysis offers a novel perspective on the evolution of intrinsically disordered proteins.
- * Reduced coevolution in disordered regions suggests different evolutionary constraints compared to ordered proteins.
- * Coevolutionary data can enhance predictions of intrinsic disorder and elucidate the functional roles of disordered protein segments.
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...
01:49Conserved Binding Sites
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 analyses the...
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 analyses the...
01:49Conserved Binding Sites
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 analyses the...
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 analyses the...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...