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  2. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  3. Unfolded protein response - Wikipedia

    en.wikipedia.org/wiki/Unfolded_protein_response

    The term protein folding incorporates all the processes involved in the production of a protein after the nascent polypeptides have become synthesized by the ribosomes.The proteins destined to be secreted or sorted to other cell organelles carry an N-terminal signal sequence that will interact with a signal recognition particle (SRP).

  4. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    Misfolded proteins can form protein aggregates or amyloid fibrils, get degraded, or refold back to its native structure. In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly.

  5. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    Heat shock proteins induced by the HSR can help prevent protein aggregation that is associated with common neurodegenerative diseases such as Alzheimer's, Huntington's, or Parkinson's disease. [8] The diagram depicts actions taken when a stress is introduced to the cell. Stress will induce HSF-1 and cause proteins to misfold.

  6. Temperature-sensitive mutant - Wikipedia

    en.wikipedia.org/wiki/Temperature-sensitive_mutant

    This results in the survival of the cell or organism, as if it were a wild type strain. In contrast, the nonpermissive temperature or restrictive temperature is the temperature at which the mutant phenotype is observed. Temperature sensitive mutations are usually missense mutations, which slightly modifies the energy landscape of the protein ...

  7. Cell cycle checkpoint - Wikipedia

    en.wikipedia.org/wiki/Cell_cycle_checkpoint

    The main mechanism of action of the cell cycle checkpoints is through the regulation of the activities of a family of protein kinases known as the cyclin-dependent kinases (CDKs), which bind to different classes of regulator proteins known as cyclins, with specific cyclin-CDK complexes being formed and activated at different phases of the cell ...

  8. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    The steps of protein synthesis include transcription, translation, and post translational modifications. During transcription, RNA polymerase transcribes a coding region of the DNA in a cell producing a sequence of RNA, specifically messenger RNA (mRNA). This mRNA sequence contains codons: 3 nucleotide long segments that code for a specific ...

  9. Proteinopathy - Wikipedia

    en.wikipedia.org/wiki/Proteinopathy

    For example, proteins that are normally unfolded or relatively unstable as monomers (that is, as single, unbound protein molecules) are more likely to misfold into an abnormal conformation. [ 5 ] [ 15 ] [ 16 ] In nearly all instances, the disease-causing molecular configuration involves an increase in beta-sheet secondary structure of the protein.