Search results
Results from the WOW.Com Content Network
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Denaturation midpoint of a protein is defined as the temperature (T m) or concentration of denaturant (C m) at which both the folded and unfolded states are equally populated at equilibrium (assuming two-state protein folding). T m is often determined using a thermal shift assay.
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.
Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses
The symbol was introduced originally in 1770 by Nicolas de Condorcet, who used it for a partial differential, and adopted for the partial derivative by Adrien-Marie Legendre in 1786. [3] It represents a specialized cursive type of the letter d , just as the integral sign originates as a specialized type of a long s (first used in print by ...
The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). [6] HSPs are found in virtually all living organisms, from bacteria to humans. Heat shock proteins are named according to their molecular weight.
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 ...
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 ...