Related Experiment Video
Updated: Jun 14, 2025
07:08
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
7.3K
Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality
Asifa Aftab1, Souradeep Sil2, Seema Nath3
1Department of Zoology, Asutosh College, (affiliated with University of Calcutta), Kolkata, 700026, India.
Journal of Molecular Evolution
|August 30, 2024
Summary
Protein multifunctionality evolves through structural flexibility, especially via intrinsically disordered proteins/regions (IDPs/IDRs). This review explores how dynamic structures enable proteins to perform multiple functions, challenging traditional views.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Structural Biology
Background:
- Understanding protein evolution reveals mechanisms for multifunctionality.
- Multifunctional proteins are crucial for complex organisms.
- Protein flexibility is key to adapting structure and function.
Purpose of the Study:
- To review the role of flexibility and structural transitions in protein multifunctionality.
- To highlight intrinsically disordered proteins/regions (IDPs/IDRs) as key drivers of multifunctionality.
- To broaden the concept of multifunctionality beyond single protein sequences.
Main Methods:
- Literature review focusing on protein structure-function relationships.
- Analysis of computational data mining and high-throughput assays.
- Exploration of molecular and intermolecular mechanisms driving protein evolution.
Main Results:
- Protein multifunctionality arises from intrinsic or adapted flexibility.
- Intrinsically disordered proteins/regions (IDPs/IDRs) exhibit fluid-like dynamics enabling disorder-to-order transitions.
- Fold-switching proteins also demonstrate structural plasticity for diverse functions.
- Multifunctionality represents a complex, multi-layered diversification, diverging from functional singularity.
Conclusions:
- Protein intrinsic disorder is a primary mechanism for achieving multifunctionality.
- Flexibility and function-driven structural transitions are central to evolved protein capabilities.
- The study broadens the scope of protein multifunctionality, emphasizing dynamic structural adaptations.
Related Concept Videos
02:18Intrinsically Disordered Proteins
17.7K
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...
17.7K
01:57Protein Complexes with Interchangeable Parts
2.5K
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...
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...
2.5K
01:22Protein Folding
117.7K
Overview
117.7K
03:03Amyloid Fibrils
9.3K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.3K
01:19Allosteric Proteins-ATCase
5.7K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
00:49Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K