reformed by heat or chemical treatment is called a thermoset elastomer. On the other hand, a thermoplastic elastomer can be molded and recycled by heat. Oxidative cross-links Many polymers undergo oxidative cross-linking, typically when exposed to atmospheric oxygen. In some cases this is undesirable and thus polymerization reactions may involve the use of an antioxidant to slow the formation of oxidative cross-links. In other cases, when formation of cross-links by oxidation is desirable, an oxidizer such as hydrogen peroxide may be used to speed up the process. The aforementioned process of applying a permanent wave to hair is one example of oxidative cross-linking. In that process the disulfide bonds are reduced, typically using a mercaptan such as ammonium thioglycolate. Following this, the hair is curled and then "neutralized". The neutralizer is typically an acidic solution of hydrogen peroxide, which causes new disulfide bonds to form under conditions of oxidation, thus permanently fixing the hair into its new configuration. It also happens for gluten which change structure of foods. In biology Proteins naturally present in the body can contain crosslinks generated by enzyme-catalyzed or spontaneous reactions. Such crosslinks are important in generating mechanically stable structures such as hair, skin, and cartilage. Disulfide bond formation is one of the most common crosslinks, but isopeptide bond formation is also common. Proteins can also be cross-linked artificially using small-molecule crosslinkers. Compromised collagen in the cornea, a condition known as keratoconus, can be treated with clinical crosslinking. In biological context crosslinking could play a role in atherosclerosis through advanced glycation end-products (AGEs), which have been implicated to induce crosslinking of collagen, which may lead to vascular stiffening. Use in protein study The interactions or mere proximity of proteins can be studied by the clever use of crosslinking agents. For example, protein A and protein B may be very close to each other in a cell, and a chemical crosslinker could be used to probe the protein–protein interaction between these two proteins by linking them together, disrupting the cell, and looking for the crosslinked proteins. A variety of crosslinkers are used to analyze subunit structure of proteins, protein interactions, and various parameters of protein function by using differing crosslinkers, often with diverse spacer arm lengths. Subunit structure is deduced, since crosslinkers bind only surface residues in relatively close proximity in the native state. Protein interactions are often too weak or transient to be easily detected, but