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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...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
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...
Three Developmental Domains01:29

Three Developmental Domains

Human development is typically examined across three main domains: physical, cognitive, and socio-emotional. These domains represent the significant areas of change and continuity throughout the lifespan, from infancy to late adulthood.
Physical Development
Physical processes, also known as maturation, encompass the biological changes that occur across an individual's life. These changes begin with genetic inheritance and continue through various stages, including growth in height and weight,...
Three-Domain System of Life01:21

Three-Domain System of Life

Ribosomal RNA (rRNA) sequence analysis revealed three distinct groups of cells: eukaryotes, bacteria, and archaea. In 1978, Carl R. Woese proposed the concept of domains, a taxonomic level above kingdoms, to differentiate these groups. He suggested that archaea and bacteria, despite their similar appearance, represent separate domains. Domains differ in rRNA, membrane lipid structure, transfer RNA, and antibiotic sensitivity.In this classification, animals, plants, and fungi belong to the...
Properties of Fourier Transform II01:24

Properties of Fourier Transform II

The Fourier Transform (FT) is an essential mathematical tool in signal processing, transforming a time-domain signal into its frequency-domain representation. This transformation elucidates the relationship between time and frequency domains through several properties, each revealing unique aspects of signal behavior.
The Frequency Shifting property of Fourier Transforms highlights that a shift in the frequency domain corresponds to a phase shift in the time domain. Mathematically, if x(t) has...

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Related Experiment Video

Updated: Jun 29, 2026

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Just how versatile are domains?

January Weiner1, Andrew D Moore, Erich Bornberg-Bauer

  • 1Institute for Evolution and Biodiversity, Evolutionary Bioinformatics Group, Westphalian Wilhelms-University, Münster, Germany. january@uni-muenster.de

BMC Evolutionary Biology
|October 16, 2008
PubMed
Summary
This summary is machine-generated.

Domain versatility, a measure of how often protein domains combine in different arrangements, is linked to domain frequency. A new index, DV I (domain versatility index), decouples versatility from frequency, revealing age independence and lower versatility in Eukaryotes.

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Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Related Experiment Videos

Last Updated: Jun 29, 2026

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
10:23

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Area of Science:

  • Evolutionary biology
  • Bioinformatics
  • Genomics

Background:

  • Protein domain arrangements are key to evolutionary innovation.
  • Domain versatility (promiscuity) describes the varied combinations domains form.
  • Previous models linked domain promiscuity to its frequency.

Purpose of the Study:

  • To investigate the relationship between domain versatility and frequency.
  • To develop a new metric, the domain versatility index (DV I), to measure versatility independent of frequency.
  • To explore biological properties associated with domain versatility.

Main Methods:

  • Analysis of domain arrangements across genomes.
  • Development and application of the domain versatility index (DV I).
  • Correlation of DV I with domain properties like age and location.

Main Results:

  • A clear relationship exists between domain promiscuity and frequency, but it varies.
  • The DV I effectively measures versatility independent of domain frequency.
  • Domains in single-domain proteins and at termini show higher DV I.
  • DV I appears age-independent, contrary to previous findings.
  • Eukaryotic domains exhibit lower versatility than previously reported.

Conclusions:

  • A random attachment process sufficiently explains observed domain arrangement distributions.
  • The DV I provides a revised perspective on domain promiscuity.
  • Understanding domain versatility aids in comprehending protein evolution and innovation.