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  2. Methods to investigate protein–protein interactions - Wikipedia

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

    Isothermal titration calorimetry (ITC), is considered as the most quantitative technique available for measuring the thermodynamic properties of proteinprotein interactions and is becoming a necessary tool for proteinprotein complex structural studies. This technique relies upon the accurate measurement of heat changes that follow the ...

  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...

    Within the field of molecular biology, a protein-fragment complementation assay, or PCA, is a method for the identification and quantification of proteinprotein 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").

  5. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    The Bradford protein assay (also known as the Coomassie protein assay) was developed by Marion M. Bradford in 1976. [1] It is a quick and accurate [2] spectroscopic analytical procedure used to measure the concentration of protein in a solution. The reaction is dependent on the amino acid composition of the measured proteins.

  6. Category:Protein–protein interaction assays - Wikipedia

    en.wikipedia.org/wiki/Category:Proteinprotein...

    Pages in category "Proteinprotein interaction assays" The following 26 pages are in this category, out of 26 total. This list may not reflect recent changes .

  7. 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]

  8. Protein methods - Wikipedia

    en.wikipedia.org/wiki/Protein_methods

    Bradford protein assay: Detection in the range of ~1 mg/mL; Biuret Test Derived Assays: Bicinchoninic acid assay (BCA assay): Detection down to 0.5 μg/mL; Lowry Protein assay: Detection in the range of 0.01–1.0 mg/mL; Fluorescamine: Quantifies proteins and peptides in solution if primary amine are present in the amino acids

  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]

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