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Types of Selection

Types of Selection

Natural selection influences the frequencies of particular alleles and phenotypes within populations in several different ways. Primarily, natural selection can be directional, stabilizing, or disruptive. Directional selection favors one extreme trait and shifts the population towards that phenotype while selecting against individuals displaying alternate traits. Stabilizing selection favors an intermediate trait with a narrow range of variation. Deviation from the optimal phenotype towards an...

Conservation of Protein Domains Over Different Proteins

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...

Gene Evolution - Fast or Slow?

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?

Gene Evolution - Fast or Slow?

Frequency-dependent Selection

Frequency-dependent Selection

When the fitness of a trait is influenced by how common it is (i.e., its frequency) relative to different traits within a population, this is referred to as frequency-dependent selection. Frequency-dependent selection may occur between species or within a single species. This type of selection can either be positive—with more common phenotypes having higher fitness—or negative, with rarer phenotypes conferring increased fitness.

Conserved Binding Sites

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...

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Related Experiment Video

Updated: May 5, 2026

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli

Published on: March 16, 2011

Directional Darwinian Selection in proteins.

David A McClellan

BMC Bioinformatics

|November 26, 2013

Summary

This summary is machine-generated.

This study introduces a novel method using amino acid properties to detect directional selection in proteins, complementing existing molecular evolution techniques. It helps reveal how natural selection shapes protein evolution.

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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

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Published on: November 7, 2012

Area of Science:

Molecular Evolution
Protein Evolution
Evolutionary Biology

Background:

Molecular evolution research employs various methods like dN/dS, HON90, and MM01.
Existing methods have limitations in fully elucidating natural selection at the molecular level.
A comprehensive understanding of molecular evolution requires complementary approaches.

Purpose of the Study:

To introduce a new, simple method for identifying and characterizing directional selection in proteins.
To utilize quantitative amino acid properties for analyzing molecular evolution.
To enhance the study of natural selection's impact on protein evolution.

Main Methods:

Analyzing inferred amino acid replacements based on single physicochemical properties.
Quantifying the amount and direction of change per amino acid replacement.
Employing a two-tailed t-test to assess the probability of zero net change in properties (H0: μ = 0).

Main Results:

Demonstrated directional selection linked to adaptive zone shifts using copepod cytochrome oxidase I data.
Showcased how convergent protein adaptations can drive convergent evolution at the organismal level.
Provided example data illustrating the application of the new method.

Conclusions:

The new method complements, rather than replaces, existing approaches in molecular evolution.
Offers a more holistic view of natural selection's role in shaping protein structure and function.
Enhances our understanding of evolutionary processes over time.