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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cis-regulatory Sequences02:02

Cis-regulatory Sequences

Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cis-regulatory Sequences02:02

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Mapping Bacterial Functional Networks and Pathways in Escherichia Coli using Synthetic Genetic Arrays
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Published on: November 12, 2012

Linear motifs: evolutionary interaction switches.

Victor Neduva1, Robert B Russell

  • 1EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

FEBS Letters
|June 10, 2005
PubMed
Summary
This summary is machine-generated.

Linear motifs are short, functional sequence patterns in proteins. This review explores their unique properties, experimental detection, and evolutionary significance compared to protein domains.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Linear motifs are short, disordered sequence patterns crucial for protein function.
  • They exhibit distinct characteristics from globular protein domains regarding binding, evolution, and detection.

Purpose of the Study:

  • To provide a comprehensive overview of linear motifs.
  • To highlight their fundamental differences from protein domains.
  • To discuss their experimental and computational identification.

Main Methods:

  • Literature review of existing research on linear motifs.
  • Comparative analysis of linear motifs and globular protein domains.
  • Discussion of experimental and computational approaches for motif discovery.

Main Results:

  • Linear motifs possess unique binding affinities and evolutionary trajectories.
  • They are often found in intrinsically disordered regions of proteins.
  • Various experimental and computational methods are employed for their identification.

Conclusions:

  • Linear motifs are critical functional elements in proteins.
  • Understanding their properties is essential for deciphering protein function and interactions.
  • Further research into linear motifs will advance molecular biology and drug discovery.