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  2. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Upon binding of an analyte to the ligand, the real-time kinetic rates (k on, k off) can be measured as changes in fluorescence intensity and the K d can be derived. This method can be used to investigate protein-protein interactions, as well as to investigate modulators of protein-protein interactions by assessing ternary complex formation.

  3. Two-hybrid screening - Wikipedia

    en.wikipedia.org/wiki/Two-hybrid_screening

    Two-hybrid screening (originally known as yeast two-hybrid system or Y2H) is a molecular biology technique used to discover proteinprotein interactions (PPIs) [1] and protein–DNA interactions [2] [3] by testing for physical interactions (such as binding) between two proteins or a single protein and a DNA molecule, respectively.

  4. Protein–protein interaction screening - Wikipedia

    en.wikipedia.org/wiki/Proteinprotein...

    Methods that screen proteinprotein interactions in the living cells. Bimolecular fluorescence complementation (BiFC) is a technique for observing the interactions of proteins. Combining it with other new techniques, dual expression recombinase based methods can enable the screening of proteinprotein interactions and their modulators. [1]

  5. Bimolecular fluorescence complementation - Wikipedia

    en.wikipedia.org/wiki/Bimolecular_fluorescence...

    Proteins that are postulated to interact are fused to unfolded complementary fragments of a fluorescent reporter protein and expressed in live cells. Interaction of these proteins will bring the fluorescent fragments within proximity, allowing the reporter protein to reform in its native three-dimensional structure and emit its fluorescent ...

  6. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Proteinprotein_interaction

    New protein was synthesized by using cell-free expression system i.e. rabbit reticulocyte lysate (RRL), and then the new protein was captured through anti-GST antibody bounded on the slide. To test proteinprotein interaction, the targeted protein cDNA and query protein cDNA were immobilized in a same coated slide.

  7. Colocalization - Wikipedia

    en.wikipedia.org/wiki/Colocalization

    Colocalization is used in real-time single-molecule fluorescence microscopy to detect interactions between fluorescently labeled molecular species. In this case, one species (e.g. a DNA molecule) is typically immobilized on the imaging surface, and the other species (e.g. a DNA-binding protein) is supplied to the solution.

  8. Today's Wordle Hint, Answer for #1273 on Friday, December 13 ...

    www.aol.com/todays-wordle-hint-answer-1273...

    If you’re stuck on today’s Wordle answer, we’re here to help—but beware of spoilers for Wordle 1273 ahead. Let's start with a few hints.

  9. Peptide mass fingerprinting - Wikipedia

    en.wikipedia.org/wiki/Peptide_mass_fingerprinting

    A typical workflow of a peptide mass fingerprinting experiment. Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. [1]