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Related Concept Videos

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...
Conservation of Protein Domains02:26

Conservation 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...
Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
In contrast, regions which code...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein 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...

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Related Experiment Video

Updated: May 12, 2026

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

Protein conformational diversity correlates with evolutionary rate.

Diego Javier Zea1, Alexander Miguel Monzon, Maria Silvina Fornasari

  • 1Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Argentina.

Molecular Biology and Evolution
|April 9, 2013
PubMed
Summary
This summary is machine-generated.

Protein conformational diversity, measured by structural differences, negatively correlates with evolutionary rate. This suggests protein flexibility influences how quickly proteins evolve.

Keywords:
conformational diversityevolutionary rateprotein evolution

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Structural Biology

Background:

  • Proteins exist as an ensemble of conformers, not a single structure.
  • Conformational diversity reflects the range of structural differences within a protein's native state.
  • Understanding protein dynamics is crucial for comprehending protein function and evolution.

Purpose of the Study:

  • To investigate the relationship between protein conformational diversity and evolutionary rate.
  • To determine if structural flexibility impacts protein divergence across species.

Main Methods:

  • Quantified conformational diversity using maximum root mean square deviation (RMSD) from the Conformational Diversity of Native State database.
  • Calculated evolutionary rates for human orthologous proteins across 16 species.
  • Analyzed the correlation between conformational diversity and evolutionary rate, controlling for protein expression levels.

Main Results:

  • A significant negative correlation was observed between protein conformational diversity and evolutionary rate.
  • This correlation remained consistent regardless of protein expression levels.
  • The magnitude and direction of this correlation were comparable to the gene expression level-evolutionary rate correlation.

Conclusions:

  • Structural constraints and protein dynamism play a role in modulating protein evolutionary divergence.
  • Increased conformational diversity may impose constraints that slow down evolutionary rates.
  • Protein flexibility is a key factor influencing the evolutionary trajectory of proteins.