Uv Cross-linking
Uv Cross-linking - Related Videos
08:40
Photo-Induced Cross-Linking of Unmodified Proteins (PICUP) Applied to Amyloidogenic Peptides
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Cited by 91 •
2009
Photo-induced cross-linking of unmodified proteins (PICUP) allows characterization of oligomer size distribution in metastable protein mixtures. We demonstrate application of PICUP to three representative amyloidogenic peptides the 40- and 42-residue forms of amyloid β-protein, and calcitonin, and a control peptide growth-hormone releasing factor.
07:02
The Preparation and Properties of Thermo-reversibly Cross-linked Rubber Via Diels-Alder Chemistry
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Cited by 3 •
2016
A simple two-step approach involving rubber modification and cross-linking yields fully reworkable, elastic rubber products.
05:56
Scleral Cross-linking Using Riboflavin and Ultraviolet-A Radiation for Prevention of Axial Myopia in a Rabbit Model
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Cited by 27 •
2016
We demonstrate the effect of scleral crosslinking with riboflavin and UVA on an axial elongation rabbit eye. Axial elongation was induced in 13 day-old New Zealand rabbits (male and female) by suturing their right eye eyelids (tarsorrhaphy).
10:04
A Filtration-based Method of Preparing High-quality Nuclei from Cross-linked Skeletal Muscle for Chromatin Immunoprecipitation
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Cited by 2 •
2017
We present a filtration-based protocol to isolate high-quality nuclei from cross-linked mouse skeletal muscle wherein we removed the need for ultracentrifugation, making it easily applicable. We show that chromatin prepared from the nuclei is suitable for chromatin immunoprecipitation and likely chromatin immunoprecipitation sequencing studies.
10:21
Protocol for HER2 FISH Using a Non-cross-linking, Formalin-free Tissue Fixative to Combine Advantages of Cryo-preservation and Formalin Fixation
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Cited by 3 •
2017
Fluorescence in-situ hybridization (FISH) is often required in combination with histopathology and molecular diagnostics for selection of therapy in personalized medicine. A novel non-cross-linking, formalin-free tissue fixative that allows high quality morphologic, molecular and FISH analyses from the same specimen by addition of a post-fixation step before FISH is presented.
FAQs
The key event is photochemical excitation: ultraviolet light raises the energy of nucleobases or an added photoactive group, creating a reactive site. If a neighboring molecule is positioned suitably at that moment, the reactive site can form a covalent bond with it. This converts a reversible association into a physically linked species that remains available for downstream analysis.
Distance and orientation strongly influence capture because the reactive site must encounter a nearby partner during irradiation. UV cross-linking therefore records molecular proximity rather than every interaction that may occur in solution. Contacts that are brief can be retained when irradiation occurs while they are present, whereas molecules that are not suitably positioned are less likely to become linked.
Using native nucleobases versus added photoactive groups changes how the reactive chemistry is introduced into the sample. Native nucleobases allow nucleic acid-containing contacts to be probed directly, while added groups provide another source of photoactivated reactivity. In either case, irradiation must occur under conditions that support bond formation without losing the interaction being investigated.
Captured material provides evidence that molecules were near one another under the irradiation conditions, not proof that the association is permanently stable. This distinction matters because UV cross-linking can preserve weak or transient contacts that might dissociate during ordinary handling. Researchers can therefore analyze the linked sample while interpreting the result as a condition-dependent proximity measurement.
A supported workflow starts with assembling or preserving the biological sample under conditions that maintain the interaction of interest, followed by ultraviolet irradiation. The resulting cross-linked material can then enter biochemical analysis, structural analysis, or sequencing-based workflows. The central procedural requirement is to irradiate while the relevant molecules remain positioned close enough for covalent bond formation.
In RNA–protein studies, irradiation can preserve contacts present between RNA molecules and associated proteins at the time of exposure. The linked material provides a stabilized sample for analyzing which molecular partners were positioned together. This is useful for investigating RNA organization and regulation, particularly when the interaction is transient and might not survive preparation for later biochemical or sequencing-based analysis.
The approach can stabilize DNA–protein or protein–protein contacts for subsequent examination of molecular organization. It also supports structural analysis by retaining neighboring components that might separate during sample handling. In biological research, these preserved associations help connect physical molecular proximity with questions about binding, organization, and regulation, while the selected downstream workflow determines how the captured material is examined.