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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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.
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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.
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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.
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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...
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A Roadmap to Domain Based Proteomics.

Carsten Kemena1, Erich Bornberg-Bauer2

  • 1Institute for Evolution and Biodiversity, University of Münster, Münster, Germany. c.kemena@uni-muenster.de.

Methods in Molecular Biology (Clifton, N.J.)
|October 10, 2018
PubMed
Summary
This summary is machine-generated.

Protein domains are key to protein evolution and function. Analyzing domain arrangements computationally aids in understanding proteomic data and reconstructing protein evolution across species.

Keywords:
Molecular evolutionProtein domain

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Area of Science:

  • Proteomics
  • Evolutionary Biology
  • Bioinformatics

Background:

  • Protein domains are fundamental units of proteins, crucial for their evolution and function.
  • The modular nature of proteins, arising from domain combinations, allows for vast diversity.
  • Computational representations like Hidden Markov Models (HMMs) enable efficient domain analysis.

Purpose of the Study:

  • To describe domain annotation methods and assess proteome annotation quality.
  • To demonstrate the use of domain functional annotations for inter-species molecular comparisons.
  • To present methods for analyzing domain content changes in protein evolution.

Main Methods:

  • Utilizing domain databases for protein domain annotation.
  • Assessing the quality of proteome annotations.
  • Applying Hidden Markov Models (HMMs) for domain identification.
  • Analyzing large-scale genomic and transcriptomic data for domain content.

Main Results:

  • Established protocols for domain annotation and quality assessment.
  • Demonstrated utility of domain analysis for comparative genomics.
  • Developed methods to characterize modular protein evolution through domain changes.

Conclusions:

  • Domain-based computational approaches are highly effective for analyzing large proteomic datasets.
  • Understanding domain arrangements provides insights into protein evolution and function.
  • This work facilitates evolutionary analyses of proteomes across diverse species.