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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...
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...
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...
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...

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Related Experiment Video

Updated: May 9, 2026

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

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

Published on: July 14, 2015

Two modes of protein sequence evolution and their compositional dependencies.

Ranjan V Mannige1

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. rvmannige@lbl.gov

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|July 16, 2013
PubMed
Summary
This summary is machine-generated.

Protein sequence composition significantly impacts its evolvability and evolutionary mode. Simulations reveal distinct "classical" and "quantum" evolution pathways, influenced by peptide properties like oiliness and charge.

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

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Last Updated: May 9, 2026

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

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

Published on: July 14, 2015

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

  • Biochemistry
  • Computational Biology
  • Evolutionary Biology

Background:

  • Protein sequence evolution drives molecular functionality essential for life.
  • Understanding how sequence composition influences protein evolution remains a key challenge in biology.

Purpose of the Study:

  • To investigate the impact of initial sequence composition on peptide and protein evolvability.
  • To identify and characterize distinct modes of sequence evolution.
  • To explore the relationship between sequence composition, evolutionary mode, and temperature response.

Main Methods:

  • Utilized lattice model simulations of directed evolution.
  • Analyzed sequence evolution under point mutation, distinguishing between
  • classical
  • and
  • quantum
  • regimes.

Main Results:

  • Peptide and protein evolvability is strongly dependent on initial sequence composition.
  • Identified two distinct evolutionary regimes:
  • classical
  • (barrier crawling) and
  • quantum
  • (barrier tunneling).
  • Oily peptides excel in the
  • classical
  • regime, while charged peptides are optimal in the
  • quantum
  • regime.
  • Temperature response in simulations parallels classical and quantum barrier crossing analogies.

Conclusions:

  • Sequence composition is a critical determinant of both the rate and mechanism of protein evolution.
  • The findings provide insights into how sequence properties can tune evolvability and optimize evolutionary pathways.