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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...
Trends in Lattice Energy: Ion Size and Charge02:54

Trends in Lattice Energy: Ion Size and Charge

An ionic compound is stable because of the electrostatic attraction between its positive and negative ions. The lattice energy of a compound is a measure of the strength of this attraction. The lattice energy (ΔHlattice) of an ionic compound is defined as the energy required to separate one mole of the solid into its component gaseous ions. For the ionic solid sodium chloride, the lattice energy is the enthalpy change of the process:
Lattice Energies of Ionic Crystals01:27

Lattice Energies of Ionic Crystals

Lattice energy represents the energy released when gaseous cations and anions combine to form an ionic solid, reflecting the strength of electrostatic interactions within the crystal. This process is fundamentally governed by Coulombic attraction between oppositely charged ions, where the potential energy varies inversely with the interionic distance and directly with the product of ionic charges. As ions approach one another, the electrostatic energy becomes increasingly negative, indicating a...
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...

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Related Experiment Video

Updated: May 13, 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

Long-term evolution is surprisingly predictable in lattice proteins.

Michael E Palmer1, Arnav Moudgil, Marcus W Feldman

  • 1Department of Biology, Stanford University, Gilbert Hall, Stanford, CA 94305-5020, USA. mepalmer@charles.stanford.edu

Journal of the Royal Society, Interface
|March 8, 2013
PubMed
Summary
This summary is machine-generated.

Natural selection can act on lineages, not just individuals. Long-term evolutionary outcomes are predictable and influenced by factors beyond short-term survival, challenging the idea of

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Related Experiment Videos

Last Updated: May 13, 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

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Area of Science:

  • Evolutionary biology
  • Computational biology
  • Molecular evolution

Background:

  • Debate exists on whether natural selection primarily targets individual organisms or higher-level entities like lineages.
  • Arguments against lineage selection include unpredictability of long-term outcomes and dominance of short-term organismal selection.

Purpose of the Study:

  • To investigate the effectiveness of long-term natural selection acting on lineages.
  • To determine if long-term evolutionary outcomes are predictable and if lineage fitness extends beyond short-term organismal fitness.

Main Methods:

  • Utilized a computational model of protein folding and binding ('lattice proteins').
  • Quantified long-term evolutionary success using k-fitness and k-survivability metrics.

Main Results:

  • Long-term evolutionary outcomes in the model were found to be surprisingly predictable.
  • Lineage fitness depends on factors beyond short-term fitness, including 'evolvability' (capacity for adaptive variation).
  • Lineages can be selected for long-term properties, even against short-term selection pressures.

Conclusions:

  • Natural selection can effectively act on lineages over long evolutionary timescales.
  • Evolutionary trajectories are predictable, and lineage fitness is influenced by multiple factors, not just immediate survival.
  • Findings suggest biological lineages may possess predictable long-term fitness, supported by in vivo observations.