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  2. Equilibrium unfolding - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_unfolding

    In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.

  3. Hydrophobic-polar protein folding model - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic-polar_protein...

    The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]

  4. 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]

  5. Vault (organelle) - Wikipedia

    en.wikipedia.org/wiki/Vault_(organelle)

    The vault or vault cytoplasmic ribonucleoprotein is a eukaryotic organelle (a structure in the cells of multicellular organisms) whose function is not yet fully understood. . Discovered and isolated by Nancy Kedersha and Leonard Rome in 1986, [2] vaults are cytoplasmic structures (outside the nucleus) which, when negative-stained and viewed under an electron microscope, resemble the arches of ...

  6. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid that is four residues earlier in the protein sequence.

  7. Beta-propeller - Wikipedia

    en.wikipedia.org/wiki/Beta-propeller

    At acidic pH the linear conformation changes to a hairpin structure such that ligand binding sites bind to the beta-propeller, preventing ligand binding. [16] [17] Beta-propeller phytases consist of a six-bladed β-propeller structure. Phytases are phosphatases that can hydrolyze the ester bonds of phytate, the major form of phosphate storage ...

  8. Depolarization - Wikipedia

    en.wikipedia.org/wiki/Depolarization

    The process of depolarization is entirely dependent upon the intrinsic electrical nature of most cells. When a cell is at rest, the cell maintains what is known as a resting potential. The resting potential generated by nearly all cells results in the interior of the cell having a negative charge compared to the exterior of the cell.

  9. Phi value analysis - Wikipedia

    en.wikipedia.org/wiki/Phi_value_analysis

    Phi value analysis assumes Hammond's postulate, which states that energy and chemical structure are correlated.Though the relationship between the folding intermediate and native state's structures may correlate that between their energies when the energy landscape has a well-defined, deep global minimum, free energy destabilizations may not give useful structural information when the energy ...