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Related Concept Videos

Conserved Binding Sites01:49

Conserved 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...
Conserved Binding Sites01:49

Conserved 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...
Intrinsically Disordered Proteins02:18

Intrinsically 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...
Intrinsically Disordered Proteins02:18

Intrinsically 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...
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 Folding01:22

Protein Folding

Overview

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

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Published on: July 14, 2015

Low-complexity regions within protein sequences have position-dependent roles.

Alain Coletta1, John W Pinney, David Y Weiss Solís

  • 1Faculty of Life Sciences, University of Manchester, Manchester M13 9PL, UK. alain.coletta@vub.ac.be

BMC Systems Biology
|April 14, 2010
PubMed
Summary

Low-Complexity Regions (LCRs) in proteins influence binding partners and functions. Their location, whether terminal or central, correlates with specific biological roles like transcription or translation.

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Published on: January 16, 2019

Area of Science:

  • Proteomics
  • Bioinformatics
  • Molecular Biology

Background:

  • Low-Complexity Regions (LCRs) are protein sequence segments with biased amino acid composition.
  • LCRs exhibit significant divergence and compositional plasticity, complicating conventional analysis.
  • The functions of most LCRs remain largely unelucidated.

Purpose of the Study:

  • To systematically investigate the functional significance of LCRs.
  • To analyze LCRs within the context of Protein-Protein Interaction (PPI) networks.
  • To explore LCRs using Gene Ontology (GO)-term analysis.

Main Methods:

  • Analysis of LCRs in relation to protein connectivity in PPI networks.
  • Investigation of LCR positional distribution within protein sequences.
  • Correlation of LCR location (terminal vs. central) with GO terms.

Main Results:

  • Proteins with LCRs generally possess more binding partners in PPI networks.
  • Terminal LCRs show a length-connectivity correlation, unlike central LCRs.
  • Central LCRs are enriched with transcription-related GO terms; terminal LCRs with translation and stress response terms.

Conclusions:

  • LCRs may participate in flexible binding crucial for specific protein functions.
  • The position of LCRs within a protein sequence influences their binding capabilities and biological roles.