Protein-decorated Dna
Protein-decorated Dna - Related Videos
03:06
From DNA to Protein
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2020
The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
05:13
Isolation of Proteins from Viral DNA-protein Complexes
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2026
Source: Dembowski, J. A., et al. Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins. J. Vis. Exp. (2017).This video demonstrates the isolation of protein–viral DNA complexes from cell nuclei using click chemistry and magnetic bead purification. The protocol involves labeling viral genomes with alkyne-modified nucleotides, biotinylation via a click reaction, and binding to streptavidin-coated magnetic beads. Following washing and heat elution, the purified...
08:53
Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
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2025
Enrichment and sequencing of protein-associated nascent DNA (eSPAN) was developed to detect the relative abundance of a chromatin-associated protein on two replicating DNA strands, thereby revealing molecular insight into chromatin replication and its coupled processes. This protocol describes eSPAN procedures in yeast and mouse embryonic stem (ES) cells.
08:51
Visualization of Surface-tethered Large DNA Molecules with a Fluorescent Protein DNA Binding Peptide
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Cited by 7 •
2016
We present an approach for visualizing fluorescent protein DNA binding peptide (FP-DBP)-stained large DNA molecules tethered on the polyethylene glycol (PEG) and avidin-coated glass surface and stretched with microfluidic shear flows.
05:42
Immunofluorescence-Based Visualization of DNA Repair Protein Interactions
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2025
In this video, we describe the immunofluorescence method to visualize the localization of the DNA repair proteins γH2AX and 53BP1 at the sites of double-strand DNA breaks in irradiated cell nuclei.
FAQs
Protein attachment can rely on either covalent coupling or specific molecular recognition. Covalent coupling creates a direct chemical connection, whereas recognition-based decoration depends on selective interactions between the molecular partners. These alternatives give researchers different ways to organize proteins on a DNA scaffold, allowing the attachment strategy to be matched to studies of DNA–protein recognition or engineered molecular functions.
DNA sequence, folding, and three-dimensional arrangement determine where attached proteins are positioned. Sequence supplies site-specific information, while folding and spatial organization shape the distances and orientations among decorated proteins. That geometric control can regulate how proteins interact with one another or with DNA, making the construct useful for examining molecular organization rather than merely displaying proteins on a molecule.
The hybrid architecture combines complementary molecular capabilities. DNA contributes information-carrying and self-assembly properties, while attached proteins contribute their own functional behavior. Organizing these capabilities within one structure can support interactions or activities that are difficult to study when DNA and proteins remain uncoordinated, particularly in research on molecular recognition, gene regulation, and organized biological systems.
By placing proteins at defined DNA sites, these constructs support investigations of DNA–protein recognition, gene regulation, and molecular organization. Their controlled arrangement helps researchers connect molecular location with interaction behavior, providing a way to examine how DNA-associated proteins are organized and how that organization may influence biological processes.
In biosensors and diagnostics, organized proteins can improve signal generation. DNA provides a structural framework, while protein placement helps arrange functional components at defined positions. This combination supports designs in which a biological interaction must produce a detectable signal, although the specific sensor or diagnostic configuration depends on the proteins selected and the DNA arrangement used.
For targeted delivery and nanotechnology, the DNA framework can organize proteins to support molecular transport or catalytic activity. Defined placement may help arrange functional components within a designed structure, while DNA self-assembly contributes to constructing that organization. The resulting platform is adaptable, with performance linked to the selected proteins and their three-dimensional arrangement.