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  2. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding must be thermodynamically favorable within a cell in order for it to be a spontaneous reaction. Since it is known that protein folding is a spontaneous reaction, then it must assume a negative Gibbs free energy value. Gibbs free energy in protein folding is directly related to enthalpy and entropy. [12]

  3. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    Numerous protein structures are the result of rational design and do not exist in nature. Proteins can be designed from scratch (de novo design) or by making calculated variations on a known protein structure and its sequence (known as protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to ...

  4. Folding funnel - Wikipedia

    en.wikipedia.org/wiki/Folding_funnel

    The diagram sketches how proteins fold into their native structures by minimizing their free energy. The folding funnel hypothesis is a specific version of the energy landscape theory of protein folding, which assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells.

  5. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    Proteins in the Hsp100/Clp family form large hexameric structures with unfoldase activity in the presence of ATP. These proteins are thought to function as chaperones by processively threading client proteins through a small 20 Å (2 nm) pore, thereby giving each client protein a second chance to fold.

  6. Category:Protein folding - Wikipedia

    en.wikipedia.org/wiki/Category:Protein_folding

    Pages in category "Protein folding" The following 21 pages are in this category, out of 21 total. This list may not reflect recent changes. ...

  7. Anfinsen's dogma - Wikipedia

    en.wikipedia.org/wiki/Anfinsen's_dogma

    Protein folding in a cell is a highly complex process that involves transport of the newly synthesized proteins to appropriate cellular compartments through targeting, permanent misfolding, temporarily unfolded states, post-translational modifications, quality control, and formation of protein complexes facilitated by chaperones.

  8. Levinthal's paradox - Wikipedia

    en.wikipedia.org/wiki/Levinthal's_paradox

    Levinthal's paradox is a thought experiment in the field of computational protein structure prediction; protein folding seeks a stable energy configuration. An algorithmic search through all possible conformations to identify the minimum energy configuration (the native state) would take an immense duration; however in reality protein folding happens very quickly, even in the case of the most ...

  9. Category:Protein folds - Wikipedia

    en.wikipedia.org/wiki/Category:Protein_folds

    Protein folds describe similar spatial arrangements of regular secondary structures in the proteins. They are helpful for structural classification of proteins . Subcategories