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  2. Protein–protein interaction - Wikipedia

    en.wikipedia.org/wiki/Proteinprotein_interaction

    The protein protein interactions are displayed in a signed network that describes what type of interactions that are taking place [74] Proteinprotein interactions often result in one of the interacting proteins either being 'activated' or 'repressed'. Such effects can be indicated in a PPI network by "signs" (e.g. "activation" or "inhibition").

  3. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Partitioning methods have many drawbacks. First, it is difficult to mimic the protein interior. [20] [21] In addition, the role of self solvation makes using free amino acids very difficult. Moreover, hydrogen bonds that are lost in the transfer to organic solvents are not reformed but often in the interior of protein. [22]

  4. Database of Interacting Proteins - Wikipedia

    en.wikipedia.org/wiki/Database_of_Interacting...

    The data stored within DIP have been curated, both manually, by expert curators, and automatically, using computational approaches that utilize the knowledge about the proteinprotein interaction networks extracted from the most reliable, core subset of the DIP data. The database was initially released in 2002.

  5. Nuclear lamina - Wikipedia

    en.wikipedia.org/wiki/Nuclear_lamina

    The nuclear lamina is a dense (~30 to 100 nm thick) fibrillar network inside the nucleus of eukaryote cells. It is composed of intermediate filaments and membrane associated proteins . Besides providing mechanical support, the nuclear lamina regulates important cellular events such as DNA replication and cell division .

  6. Interactome - Wikipedia

    en.wikipedia.org/wiki/Interactome

    In molecular biology, an interactome is the whole set of molecular interactions in a particular cell.The term specifically refers to physical interactions among molecules (such as those among proteins, also known as proteinprotein interactions, PPIs; or between small molecules and proteins [1]) but can also describe sets of indirect interactions among genes (genetic interactions).

  7. Macromolecular crowding - Wikipedia

    en.wikipedia.org/wiki/Macromolecular_crowding

    Added to this mix are various forms of RNA and the cell's DNA chromosome, giving a total concentration of macromolecules of between 300 and 400 mg/ml. [3] In eukaryotes the cell's interior is further crowded by the protein filaments that make up the cytoskeleton, this meshwork divides the cytosol into a network of narrow pores. [9]

  8. Protein–protein interaction prediction - Wikipedia

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

    Proteinprotein interaction prediction is a field combining bioinformatics and structural biology in an attempt to identify and catalog physical interactions between pairs or groups of proteins. Understanding proteinprotein interactions is important for the investigation of intracellular signaling pathways, modelling of protein complex ...

  9. TIM barrel - Wikipedia

    en.wikipedia.org/wiki/TIM_barrel

    Cyan lines depict an example backbone β-barrel hydrogen bonding network. Note that side-chain hydrogen bonding networks are not depicted here. Interior β-barrel residues (pore residues) display a 4-fold geometric symmetry, despite emerging from an 8-strand β-barrel. This symmetry is illustrated as two example "layers" in red and blue.