Chemically Induced Dimerization
Chemically Induced Dimerization - Related Videos
08:52
Chemical Dimerization-Induced Protein Condensates on Telomeres
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Cited by 10 •
2021
This protocol illustrates a chemically induced protein dimerization system to create condensates on chromatin. The formation of promyelocytic leukemia (PML) nuclear body on telomeres with chemical dimerizers is demonstrated. Droplet growth, dissolution, localization and composition are monitored with live cell imaging, immunofluorescence (IF) and fluorescence in situ hybridization (FISH).
10:17
Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Cited by 3 •
2020
Creating chemically induced protein dimerization systems with desired affinity and specificity for any given small molecule ligand would have many biological sensing and actuation applications. Here, we describe an efficient, generalizable method for de novo engineering of chemically induced dimerization systems via the stepwise selection of a phage-displayed combinatorial single-domain antibody library.
10:39
Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Cited by 43 •
2014
We present a protocol of how to collect and process electron cryo-tomograms of whole mitochondria. The technique provides detailed insights into the structure, function, and organization of large membrane protein complexes in native biological membranes.
03:23
Assessment of Chemical-Induced Colitis via Immunohistochemical Analysis of Colon Tissue Sections
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2025
This video demonstrates the assessment of chemical-induced colitis via immunohistochemical staining of mouse colon tissue. In a stained tissue section, the presence of a large number of immune-responsive cells in the damaged tissue represents the infiltration of immune cells during colitis.
10:44
Isolating Free Carbenes, their Mixed Dimers and Organic Radicals
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Cited by 5 •
2019
We present protocols for the isolation of stable heterocyclic carbenes. The synthesis of a cyclic (alkyl)(amino) carbene (CAAC) and an N-heterocyclic carbene (NHC) is demonstrated using filter cannulas and Schlenk technique. We furthermore present the synthesis of the related oxygen-sensitive, electron-rich mixed “Wanzlick dimer” and the reduced stable organic radical.
FAQs
Ligand binding to one engineered protein domain can stabilize its association with a second domain when both recognize the same chemical inducer. This creates controlled proximity between linked proteins. In a biochemical experiment, that induced proximity can alter the behavior of a signaling component, enzyme, or localization construct, depending on the proteins selected for the system.
Reversible control allows researchers to examine protein interactions as timed events rather than permanent changes. Adding the inducer can trigger association, while removing it can reverse the dimerization. This capability helps investigators study dynamic protein interactions and determine how quickly signaling, enzyme activity, or protein localization responds to changes in proximity.
Engineered binding domains provide the recognition sites for the chemical inducer, while fusion proteins connect those domains to the cellular proteins being regulated. Their arrangement determines which proteins are brought together after ligand binding. This design lets researchers direct the induced proximity toward signaling pathways, enzymes, localization targets, or synthetic cellular components.
An application generally begins by selecting engineered binding domains that recognize the chosen chemical inducer and attaching them to proteins of interest as fusion proteins. Researchers then introduce the system into cells, add the inducer to promote association, and remove it when reversal is needed. The resulting changes in protein behavior can then be examined.
By bringing selected signaling proteins into proximity, the system can alter when and where components of a pathway interact. Researchers can therefore use inducer-dependent association to investigate pathway behavior under controlled timing. This approach is especially useful when the goal is to connect a change in protein proximity with a downstream signaling response inside cells.
Fusion proteins can be designed so that inducer-dependent association changes an enzyme's proximity to another protein or alters where a protein is positioned in the cell. Measuring the resulting functional or localization changes helps connect molecular positioning with biochemical behavior. The same strategy supports controlled examination of protein function without relying only on static interactions.
The approach supports synthetic cellular circuits in which a chemical input controls a defined protein interaction. It also provides a research platform for studying dynamic protein interactions and for designing controllable therapeutic systems. Because association can be triggered and reversed, investigators can relate the timing of the chemical input to changes in cellular activity.