Proteins are formed when amino acids join together through peptide bonds, which is why they are also called polypeptides. Peptide bonds between amino acids are formed by a process called dehydration synthesis. The conformation of a protein depends on the physical and chemical conditions of the surrounding environment such as pH and temperature. The amino acid sequence of a protein (a simple organic compound containing both a carboxyl group and an amino group) determines how it functions. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The tendency of nonpolar molecules in a polar solvent to interact with each other is called the hydrophobic effect. Proteins have hydrophobic amino acids, such as glycine, clustered together within the protein. They are amino acids with hydrophobic side chains that become clusters at the center of a protein as a polypeptide folds into its functional form. Say no to plagiarism. Get a tailor-made essay on "Why Violent Video Games Shouldn't Be Banned"? Get Original Essay Hydrogen bonding between amino groups and carboxyl groups in a protein sheet causes certain folding patterns to occur. These hydrogen bonds cause the chain of amino acids to bend or coil. This can involve two specific forms. An alpha helix is ​​formed when hydrogen bonds form in a chain causing a spiral pattern. Beta sheets form when chains parallel to each other connect to create a pleated shape. These folding patterns constitute the secondary structure of a protein. Van der Waals interactions are defined as constantly evolving “hot spots of positive/negative charge” that allow atoms to stick together, due to the constant, “asymmetric” movement of electrons ( 1). In protein structures, this means that a protein must have a particular shape to function properly. Van der Waals forces are able to do this because “slight differences in the dipole moment of two parts of the protein chain” allow these two parts to connect together (3). It is thanks to this connection that proteins are able to fold into the different structures that allow them to function in the organism they occupy. Van der Waals interactions also contribute to the strength of the hydrophobic effect, because nonpolar atoms are particularly favored in this type of interaction (2). Prions are proteins found on the plasma membrane (the membrane that surrounds a cell and defines its physical structure). confine). In mammals, prions are found in the highest concentration in the cells of the central nervous system. Infection of normal cells can occur when an aberrant prion serves as a template for the folding of a normal prion into a new aberrant prion. At least one other protein is believed to be involved: protein X, which has not yet been identified. This protein is thought to mediate folding from a normal prion to an abnormal one. When proteins are synthesized inside a cell, there are other special proteins (known as chaperones) that help in this process. Chaperones are proteins that bind to the newly synthesized protein or protein subunit, to ensure that the protein is properly folded into its secondary or tertiary structure. It has been hypothesized that Protein X is a type of chaperone. Further studies are needed before we can determine whether the disease is caused by the lack of normal prions or the presence of aberrant prions. This is just one of the questions researchers are currently trying to answer. There is currently a lot of research going on into the transformation mechanism.