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  2. Methods to investigate protein–protein interactions - Wikipedia

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

    Chemical cross-linking followed by high mass MALDI mass spectrometry can be used to analyze intact protein interactions in place before trying to isolate/identify interacting proteins. This method detects interactions among non-tagged proteins and is available from CovalX. SPINE (Strepprotein interaction experiment) [10] uses a combination of ...

  3. Protein–lipid interaction - Wikipedia

    en.wikipedia.org/wiki/Proteinlipid_interaction

    Proteinlipid 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?

  4. Protein-fragment complementation assay - Wikipedia

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

    Interaction between the bait and the prey proteins brings the fragments of the reporter protein in close proximity to allow them to form a functional reporter protein whose activity can be measured. This principle can be applied to many different reporter proteins and is also the basis for the yeast two-hybrid system , an archetypical PCA assay.

  5. Proximity labeling - Wikipedia

    en.wikipedia.org/wiki/Proximity_labeling

    Mitochondrial outer membrane proteins are identified via proximity labeling. Enzyme-catalyzed proximity labeling (PL), also known as proximity-based labeling, is a laboratory technique that labels biomolecules, usually proteins or RNA, proximal to a protein of interest. [1]

  6. Tandem affinity purification - Wikipedia

    en.wikipedia.org/wiki/Tandem_Affinity_Purification

    Tandem affinity purification (TAP) is an immunoprecipitation-based purification technique for studying proteinprotein interactions.The goal is to extract from a cell only the protein of interest, in complex with any other proteins it interacted with.

  7. 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]

  8. Protein microarray - Wikipedia

    en.wikipedia.org/wiki/Protein_microarray

    A protein microarray (or protein chip) is a high-throughput method used to track the interactions and activities of proteins, and to determine their function, and determining function on a large scale. [1] Its main advantage lies in the fact that large numbers of proteins can be tracked in parallel.

  9. Lipid-anchored protein - Wikipedia

    en.wikipedia.org/wiki/Lipid-anchored_protein

    The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. [1] [2] They are a type of proteolipids. The lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is attached. [2]