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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]
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.
Hemichromes can be classified in two main categories: reversible and irreversible. Reversible hemichromes (Hch-1) have the ability to return to their native formation (hemoglobin). Some hemichromes can be reduced to the high-spin state of deoxyhemoglobin , while others are first being reduced to hemochromes (FeII) and then to deoxyhemoglobin ...
The greatest disadvantage to isoelectric point precipitation is the irreversible denaturation caused by the mineral acids. For this reason isoelectric point precipitation is most often used to precipitate contaminant proteins, rather than the target protein.
Cellular proteins are held in a relatively constant pH in order to prevent changes in the protonation state of amino acids. [24] If the pH drops, some amino acids in the polypeptide chain can become protonated if the pka of their R groups is higher than the new pH. Protonation can change the charge these R groups have.
A and B can react to form C and D or, in the reverse reaction, C and D can react to form A and B. This is distinct from a reversible process in thermodynamics. Weak acids and bases undergo reversible reactions. For example, carbonic acid: H 2 CO 3 (l) + H 2 O (l) ⇌ HCO 3 − (aq) + H 3 O + (aq).
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 ...
And there is an obvious paradox: in reversible enzymatic reaction if the active site perfectly fits the substrates then the backward reaction will be slowed since products cannot fit perfectly into the active site. So conformational distortion was introduced and argues that both active site and substrate can undergo conformational changes to ...