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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Complex Numbers01:29

Complex Numbers

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The real number system cannot represent the square root of a negative number, which restricts solutions for certain equations, such as quadratics with negative discriminants. To address this, the complex number system was developed, introducing the imaginary unit i, where i = √(-1). This extension allows for the representation of all roots, including those involving negative radicands.A complex number is written in the form x + yi, where x and y are real numbers. Here, x represents the...
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Formation of Complex Ions03:45

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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
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Complex Power01:14

Complex Power

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Power engineers have introduced the concept of complex power to determine the cumulative effect of parallel loads. This idea plays a crucial role in power analysis because it encompasses all the details related to the power consumed by a specific load.
Complex power is defined as the multiplication of the voltage and the complex conjugate of the current. The magnitude of this power, known as apparent power, is measured in volt-amperes (VA). Notably, the angle of the complex power equates to the...
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Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

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In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
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Related Experiment Video

Updated: Feb 3, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
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Complex Portal 2018: extended content and enhanced visualization tools for macromolecular complexes.

Birgit H M Meldal1, Hema Bye-A-Jee1, Lukáš Gajdoš2

  • 1European Bioinformatics Institute (EMBL-EBI), European Molecular Biology Laboratory, Wellcome Genome Campus, Hinxton, Cambridgeshire CB10 1SD, UK.

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Summary

The Complex Portal database now offers improved FAIR data compliance with stable identifiers and versioning for macromolecular complexes. Enhanced features include 3D structure visualization and a downloadable yeast complexome.

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Area of Science:

  • Biochemistry
  • Bioinformatics
  • Systems Biology

Background:

  • The Complex Portal is a curated database for macromolecular complexes.
  • It links to external resources like PDB and Reactome for detailed data.
  • Previous versions lacked robust data accessibility and FAIR data principles compliance.

Purpose of the Study:

  • To enhance the Complex Portal database with improved FAIR data principles compliance.
  • To provide better accessibility and visualization of protein complex data.
  • To offer a comprehensive view of the yeast complexome.

Main Methods:

  • Implemented complex-specific, stable identifiers with versioning.
  • Developed a new website using a component-based JS front-end framework.
  • Integrated APIs from linked services for data visualization and import.

Main Results:

  • Protein complex data is now available from 20 species in standard formats (PSI-XML, MI-JSON, ComplexTAB).
  • An improved REST API facilitates data access.
  • New website features enable visualization of 3D structures, pathways, and co-expression data.
  • A draft of the Saccharomyces cerevisiae complexome is available for download.

Conclusions:

  • The updated Complex Portal significantly improves data accessibility and usability for researchers.
  • Enhanced features support deeper understanding of protein complex organization and function.
  • The database advances the study of macromolecular complexes and systems biology.