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  2. Protein–lipid interaction - Wikipedia

    en.wikipedia.org/wiki/Proteinlipid_interaction

    Protein–lipid interaction is the influence of membrane proteins on the lipid physical state or vice versa.. The questions which are relevant to understanding of the structure and function of the membrane are: 1) Do intrinsic membrane proteins bind tightly to lipids (see annular lipid shell), and what is the nature of the layer of lipids adjacent to the protein?

  3. Methods to investigate protein–protein interactions - Wikipedia

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

    Bio-layer interferometry (BLI) is a label-free technology for measuring biomolecular interactions [27] [28] (protein:protein or protein:small molecule). It is an optical analytical technique that analyzes the interference pattern of white light reflected from two surfaces: a layer of immobilized protein on the biosensor tip, and an internal ...

  4. Bicinchoninic acid assay - Wikipedia

    en.wikipedia.org/wiki/Bicinchoninic_acid_assay

    BCA protein assay in a 96 well plate. The bicinchoninic acid assay (BCA assay), also known as the Smith assay, after its inventor, Paul K. Smith at the Pierce Chemical Company, [1] now part of Thermo Fisher Scientific, is a biochemical assay for determining the total concentration of protein in a solution (0.5 μg/mL to 1.5 mg/mL), similar to Lowry protein assay, Bradford protein assay or ...

  5. Protein-fragment complementation assay - Wikipedia

    en.wikipedia.org/wiki/Protein-fragment...

    Within the field of molecular biology, a protein-fragment complementation assay, or PCA, is a method for the identification and quantification of protein–protein interactions. In the PCA, the proteins of interest ("bait" and "prey") are each covalently linked to fragments of a third protein (e.g. DHFR, which acts as a "reporter").

  6. Proximity extension assay - Wikipedia

    en.wikipedia.org/wiki/Proximity_extension_assay

    The proximity extension assay (PEA) is a method for detecting and quantifying the amount of many specific proteins present in a biological sample such as serum or plasma. [1] The method is used in the research field of proteomics , specifically affinity proteomics, [ 2 ] where in one searches for differences in the abundance of many specific ...

  7. Microscale thermophoresis - Wikipedia

    en.wikipedia.org/wiki/Microscale_thermophoresis

    between any kind of biomolecules [1] including proteins, DNA, [2] RNA, [3] peptides, [4] small molecules, [5] fragments [6] and ions; for interactions with high molecular weight complexes, large molecule assemblies, even with liposomes, [7] vesicles, nanodiscs, [8] nanoparticles [9] and viruses

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  9. Fluorescence recovery after photobleaching - Wikipedia

    en.wikipedia.org/wiki/Fluorescence_recovery...

    Photodestroying the GFP, and then watching the repopulation into the bleached area can reveal information about protein interaction partners, organelle continuity and protein trafficking. [ 4 ] If after some time the fluorescence doesn't reach the initial level anymore, then some part of the fluorescence is caused by an immobile fraction (that ...

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