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Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. The steps of protein synthesis include transcription, translation, and post translational modifications.
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.
Moist heat causes destruction of micro-organisms by denaturation of macromolecules, primarily proteins. Destruction of cells by lysis may also play a role. While "sterility" implies the destruction of free-living organisms which may grow within a sample, sterilization does not necessarily entail destruction of infectious matter.
Heat shock proteins induced by the HSR can help prevent protein aggregation that is associated with common neurodegenerative diseases such as Alzheimer's, Huntington's, or Parkinson's disease. [8] The diagram depicts actions taken when a stress is introduced to the cell. Stress will induce HSF-1 and cause proteins to misfold.
Dry heat sterilization of an object is one of the earliest forms of sterilization practiced. It uses hot air that is either free from water vapor or has very little of it, where this moisture plays a minimal or no role in the process of sterilization.
Since proteins typically aggregate upon denaturation (or form fibrils) the detected species size will go up. This is label-free and independent of specific residues in the protein or buffer composition. The only requirement is that the protein actually aggregates/fibrillates after denaturation and that the protein of interest has been purified.
Like other biomolecules, proteins can also be broken down by high heat alone. At 250 °C, the peptide bond may be easily hydrolyzed, with its half-life dropping to about a minute. [29] [32] Protein may also be broken down without hydrolysis through pyrolysis; small heterocyclic compounds may start to form upon