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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.
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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Protein Folding01:22

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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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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: Jul 24, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Voltage-calibrated, finely tunable protein assembly.

Yin-Chen Lin1,2, Eloise Masquelier1,3, Yahya Al Sabeh1,4

  • 1Institute for Collaborative Biotechnologies, University of California, Santa Barbara, CA 93106, USA.

Journal of the Royal Society, Interface
|July 5, 2023
PubMed
Summary
This summary is machine-generated.

Researchers electrically controlled reflectin protein assembly, mimicking natural squid color changes. This discovery offers new ways to manipulate and observe protein dynamics using electrical signals.

Keywords:
electrochemistryprotein assemblyreflectinspectroscopy

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Reflectin proteins in squid enable dynamic color changes for camouflage and communication.
  • Neuronally triggered phosphorylation controls reflectin assembly and color modulation.

Purpose of the Study:

  • To investigate electrochemical control of reflectin A1 protein assembly.
  • To establish a parallel between physiological phosphorylation and electrochemical reduction in controlling protein assembly size.

Main Methods:

  • Electrochemical reduction of reflectin A1.
  • Simultaneous analysis using in situ dynamic light scattering, circular dichroism, and UV absorbance spectroscopies.

Main Results:

  • Electrochemical reduction triggered voltage-calibrated, proportional, and cyclable control over reflectin A1 assembly size.
  • Assembly size correlated with applied potential, suggesting a link to reflectin's dynamic arrest mechanism.

Conclusions:

  • Electrochemical methods can precisely control reflectin assembly, mirroring biological processes.
  • This provides a novel platform for electrokinetically controlling and observing macromolecular systems and their dynamics.