Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Detergent Purification of Membrane Proteins

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

<i>Trichomonas vaginalis</i> PPi-dependent phosphofructokinase structures reveal a non-canonical nucleotide binding site.

bioRxiv : the preprint server for biology·2026

Same author

Dual-Mode Native Mass Spectrometry Screening Identifies Ginsenoside Ligands of 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase (HPPK).

Molecules (Basel, Switzerland)·2026

Same author

Crystal structure of Plasmodium vivax macrophage migration inhibitory factor.

Acta crystallographica. Section F, Structural biology communications·2026

Same author

Benchmarking Hi-C scaffolders using reference genomes and de novo assemblies.

Genome biology·2026

Same author

Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27.

Acta crystallographica. Section F, Structural biology communications·2026

Same author

Crystal structure of a short-chain dehydrogenase from Brucella ovis with apo and coenzyme NAD<sup>+</sup>-bound protomer chains.

Acta crystallographica. Section F, Structural biology communications·2025

Same journal

Genetic Impacts on Variability of Body Fat Distribution Uncover Gene-Environment and Gene-Gene Interactions.

bioRxiv : the preprint server for biology·2026

Same journal

16S ribosomal RNA modification drives transcript-specific translation efficiency.

bioRxiv : the preprint server for biology·2026

Same journal

FlcE latches onto the FliL-stator complex to turbocharge flagellar motility in <i>Borrelia burgdorferi</i>.

bioRxiv : the preprint server for biology·2026

Same journal

Synaptic pruning, myelination and the emergence of psychiatric disorders in late adolescence.

bioRxiv : the preprint server for biology·2026

Same journal

Structural and functional insights into the Rcs phosphorelay.

bioRxiv : the preprint server for biology·2026

Same journal

The structural basis of RanGAP1 regulation and catalysis in nuclear transport.

bioRxiv : the preprint server for biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Apr 11, 2026

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Published on: December 15, 2017

Automated extraction and optimization of protein purification protocols using multi-agent large language models.

Jeffery Ye^1,2, Amy DeRocher^1,2, Monique Khim^1,2

¹Seattle Structural Genomics Center for Infectious Disease, 1916 Boren Avenue, Seattle, WA 98101 USA.

Biorxiv : the Preprint Server for Biology

|April 10, 2026

Summary

This summary is machine-generated.

This study introduces a multi-agent Large Language Model (LLM) system to automate protein purification protocol design. The system streamlines literature reviews and optimization, reducing analysis time from hours to minutes for biomedical research.

More Related Videos

Automated Robotic Liquid Handling Assembly of Modular DNA Devices

Automated Robotic Liquid Handling Assembly of Modular DNA Devices

Published on: December 1, 2017

Shotgun Proteomics Sample Processing Automated by an Open-Source Lab Robot

Shotgun Proteomics Sample Processing Automated by an Open-Source Lab Robot

Published on: October 28, 2021

Related Experiment Videos

Last Updated: Apr 11, 2026

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Generic Protocol for Optimization of Heterologous Protein Production Using Automated Microbioreactor Technology

Published on: December 15, 2017

Automated Robotic Liquid Handling Assembly of Modular DNA Devices

Automated Robotic Liquid Handling Assembly of Modular DNA Devices

Published on: December 1, 2017

Shotgun Proteomics Sample Processing Automated by an Open-Source Lab Robot

Shotgun Proteomics Sample Processing Automated by an Open-Source Lab Robot

Published on: October 28, 2021

Area of Science:

Biotechnology
Computational Biology
Biochemistry

Background:

Protein purification is critical for biomedical research but often fails.
Manual optimization of purification protocols is time-intensive and complex.
Existing methods lack efficiency in handling proteins with low stability or solubility.

Purpose of the Study:

To automate the creation and optimization of protein purification protocols using a multi-agent Large Language Model (LLM) system.
To improve the success rate of producing high-concentration, high-purity protein samples.
To streamline the manual processes involved in sequence similarity searches, literature reviews, and protocol comparison.

Main Methods:

A multi-agent LLM system was developed to operate within a constrained workflow.
The system identifies analogous proteins and extracts purification methodologies from scientific literature.
It cross-references successful and failed protocols to generate optimization recommendations.

Main Results:

The system demonstrated high accuracy in extracting purification protocols from literature.
It generated scientifically sound and expert-validated optimization recommendations.
Complex analysis time was reduced from hours to minutes for target proteins.

Conclusions:

LLM agents can effectively automate and streamline complex wet-lab workflows like protein purification.
The developed system enhances methodological transparency and reproducibility in scientific research.
Programmatic open access to scientific literature, particularly primary citations, is crucial for advancing LLM-based scientific workflows.