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The Myths of Protein Folding: How Do They Determine How Life Works?
In the field of biochemistry, protein folding and denaturation are key to the operation of life. When a protein or nucleic acid loses its original folded structure due to various factors, it is called denaturation. This change may be caused by the application of external pressure or compounds, such as strong acids or bases, high concentrations of inorganic salts, organic solvents such as alcohol or chloroform, shaking and radiation, or the effects of heat.
"If the proteins in cells are denatured, it will lead to the interruption of cell activities and may even cause cell death."
Protein denaturation results in a variety of characteristics, including conformational changes, loss of solubility, and aggregation due to exposure of hydrophobic groups. When proteins lose their three-dimensional structure, they can no longer function properly. Therefore, proper protein folding is crucial for whether a globular or membrane protein can perform its task correctly.
Examples of transgender
Many examples from everyday life can help to understand transgenderism. For example, some proteins become denatured when food is cooked. Hard-boiled eggs become firmer, while cooked meat becomes firmer. In addition, raw egg whites turn into an opaque solid when heated, which is a classic example of denaturation. Similarly, putting raw fish or shellfish in an acidic citrus marinade can also cause protein denaturation through "chemical cooking."
Background of protein denaturation
Proteins are polymers composed of amino acids. The protein synthesis process is controlled by ribosomes, which "read" the RNA and assemble the required amino acid sequence according to the genetic instructions encoded in the gene. The newly synthesized protein chain undergoes posttranslational modification, a process in which elements such as copper, zinc, or iron may be added.
After undergoing these post-translational modifications, proteins begin to fold, usually spontaneously or with the help of enzymes. The final shape of a protein determines how it interacts with its environment. The protein folding process involves a large number of weak internal interactions (such as hydrophobic, electrostatic and van der Waals interactions) as well as protein-solvent interactions.
"This process is deeply affected by the environmental conditions, including temperature, salinity, pressure and other factors."
Degeneration and loss of function
For biological matrices, most lose their biological functions when denatured. Taking enzymes as an example, when an enzyme is denatured, the substrate can no longer bind to the active site, and the amino acid residues used to stabilize the substrate's transition state are no longer in viable positions. This denaturation process and the consequent loss of activity can be measured by a variety of techniques, including double polarization interferometry, circular dichroism spectroscopy, and mass sensitivity resonance.
The impact of heavy metals
Heavy metals have been shown to affect the function and activity of proteins. These metals mainly include transition metals and some semimetals. When these metals interact with folded proteins, they will hinder their biological activity and interfere with the normal function of the protein in a variety of ways.
Reversibility and irreversibility of denaturation
In many cases, protein denaturation is reversible, and when the denaturing factor is removed, the protein can return to its original form. However, sometimes denaturation is irreversible, which is usually a kinetic irreversibility because the folded protein possesses a lower free energy relative to the unfolded state.
Summary
Understanding protein denaturation is not only a part of biochemical research, but also has important significance for many technologies such as polymerase chain reaction (PCR) and nucleic acid electrophoresis. As we explore more deeply the workings of these tiny building blocks of life, can we imagine what life would be like without the proper folding of these proteins?
