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  2. Anfinsen's dogma - Wikipedia

    en.wikipedia.org/wiki/Anfinsen's_dogma

    Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology. It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence . [ 1 ]

  3. 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.

  4. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.

  5. Thermostability - Wikipedia

    en.wikipedia.org/wiki/Thermostability

    Crystal structure of β-glucosidase from Thermotoga neapolitana (PDB: 5IDI).Thermostable protein, active at 80°C and with unfolding temperature of 101°C. [1]In materials science and molecular biology, thermostability is the ability of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative ...

  6. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Thermodynamic stability of proteins represents the free energy difference between the folded and unfolded protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation. Protein denaturation may result in loss of function, and loss of native state.

  7. Transmembrane protein - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_protein

    Stability of beta barrel (β-barrel) transmembrane proteins is similar to stability of water-soluble proteins, based on chemical denaturation studies. Some of them are very stable even in chaotropic agents and high temperature. Their folding in vivo is facilitated by water-soluble chaperones, such as protein Skp. It is thought that β-barrel ...

  8. Biological thermodynamics - Wikipedia

    en.wikipedia.org/wiki/Biological_thermodynamics

    Biological thermodynamics (Thermodynamics of biological systems) is a science that explains the nature and general laws of thermodynamic processes occurring in living organisms as nonequilibrium thermodynamic systems that convert the energy of the Sun and food into other types of energy. The nonequilibrium thermodynamic state of living ...

  9. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    Sometimes, HSP70 is unable to effectively aid a protein in reaching its final 3-D structure; The main reason being the thermodynamic barriers for folding are too high for the chaperone to meet. [23] Because the intracellular space is very crowded, sometimes proteins need an isolated space to prevent aberrant interactions between other proteins ...