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Related Concept Videos

Protein Complex Assembly

Protein Complex Assembly

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...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

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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Assembly of Cytoskeletal Filaments

Assembly of Cytoskeletal Filaments

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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Related Experiment Video

Updated: Apr 2, 2026

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

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

Published on: July 17, 2019

Protein Assembly in Serum and the Differences from Assembly in Buffer.

John J Hill¹, Thomas M Laue²

¹Amgen, Seattle, Washington, USA.

Methods in Enzymology

|September 29, 2015

Summary

This summary is machine-generated.

Analytical ultracentrifugation with fluorescence detection reveals distinct protein interactions in serum compared to dilute solutions. This method aids in understanding therapeutic activity and pharmacokinetics in vivo.

Keywords:

Analytical ultracentrifugation Antibody Assembly Binding Clusters Concentrated solution Confined Crowded Fluorescence detection system Osteoprotegerin RANKL Sedimentation velocity Serum

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Area of Science:

Biochemistry
Analytical Chemistry
Pharmacology

Background:

Protein-binding interactions are crucial for biological processes.
Characterizing these interactions in complex biological fluids like serum is challenging.
Understanding in vivo behavior is key for therapeutic development.

Purpose of the Study:

To demonstrate analytical ultracentrifugation (AUC) coupled with fluorescence detection for characterizing protein interactions.
To compare protein-binding and assembly states in dilute solutions versus serum.
To highlight the utility of this method for in vivo pharmacokinetic and therapeutic activity studies.

Main Methods:

Analytical ultracentrifugation (AUC) utilized for separating and analyzing biomolecules.
Fluorescence detection system integrated with AUC for sensitive monitoring.
Experiments conducted in both dilute buffer solutions and serum (a complex biological matrix).

Main Results:

Protein-binding and assembly states in serum were significantly different from those in dilute buffers.
Observed differences for endogenous protein ligands and an antibody inhibitor.
Demonstrated the capability of the method to detect these variations.

Conclusions:

AUC with fluorescence detection is a powerful tool for studying protein interactions in complex environments like serum.
This approach provides insights into how crowding and solution composition affect protein behavior.
The method can inform research on therapeutic efficacy and in vivo pharmacokinetics.