The concept of proteins having important biological functions emerged in the 19th century. In 1838, French chemist Anselme Payen isolated the first enzyme, diastase, which is now known as amylase, from malt. Further research revealed that enzymes were in fact proteins that could catalyze biochemical reactions without being used up in the process. By the early 1900s, scientists knew proteins played critical roles as enzymes, hormones, antibodies and structural components of cells and tissues. However, it was not until the middle of the 20th century that our understanding of proteins and their functions really took off.

Antibodies, also known as immunoglobulins, are Y-shaped glycoproteins produced by B-cells of the immune system in response to antigens like viruses or bacteria. They recognize and latch onto foreign substances to neutralize and eliminate pathogens from the body. Different classes of antibodies include IgA, IgD, IgE, IgG and IgM.

Functional Protein development of new techniques like X-ray crystallography and the emergence of molecular biology in the 1950s and 1960s, scientists were able to determine the exact structure and sequences of different proteins. This opened doors to unravel how proteins folded into their three-dimensional shapes and how even small changes in their amino acid sequences could result in large differences in structure and function. Landmark discoveries in these years included the cracking of the structure of myoglobin by John Kendrew in 1958 and the determination of the α-helical structure of keratin by Linus Pauling and Robert Corey in 1951.

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