Introduction: Linus Pauling was one of the world’s most notable scientists.
He was a theoretical physical chemist who overtime, became the original person to have received two unshared Nobel Prizes. Known as one of the world’s most protruding scientist’s humanitarians, Pauling for years was recognised as being the most perceptible, vocal, and accessible American scientists. His distinct attire became his trademark, a black beret worn over a shock of curly white hair, along with a pair of blue eyes that conveyed his penetrating curiosity toward stimulating areas.
His evaluations of perplexing medical and scientific information were what shaped Pauling and his career as well as contributing greatly to the study of chemistry itself. Linus Pauling was born in Portland, Oregon, on February 28, 1901. Linus received his early education in Oregon and finished in 1922 with a bachelor’s degree in chemical engineering. In 1925 Pauling received a Ph.D. in chemistry and mathematical physics. He was then granted a Guggenheim Fellowship which he then pursued in Europe, working with physicists whom were exploring the implications of quantum mechanics for atomic structure. In 1954 Pauling was awarded a Nobel Prize in chemistry and went on to receive a further 20 awards such as Nobel Peace Prize and a National medal of science for physical science that attributed to his outstanding discoveries.
In the final years of Pauling’s life, he began to lessen his formerly frequent travel and lecturing. Pauling continued to publish articles, however, this soon became less frequent as he was diagnosed with prostate cancer in 1991. After undergoing various surgeries, the cancer spread to his liver and he passed away at home on August 19th, 1994.During the 1950’s, Linus Pauling discovered the spiral structure of proteins which ultimately spawned his career, directing it towards molecular biology. Pauling’s discovery contributed towards James Watson and Francis Crick’s breakthrough of the double helix, known as a pair of parallel helices intertwined about a common axis, particularly that of a DNA molecule.
In 1922 Pauling then went on to study a method identified as X-ray crystallography “which is a technique used for determining the atomic molecular structure of a crystal” (Taton, 1964, p.289). X-ray crystallography was initially discovered by scientist W.
H. Bragg. However, Pauling was quick to infer rules of understanding the concept of X-ray which allowed him to figure out the shape of protein. After developing an illness in 1948 that confined Pauling to bed, he was able to deliberate Astbury’s idea that “globular proteins are made up of polypeptide chains that are folded to make balls”, (Gribbin, 2002, p. 561). From his previous knowledge of X-ray crystallography, Pauling was able to further grasp the concept of how amino acids fit together to make proteins (Gribbin, 2002).
After extensive use of paper models and working with jigsaw puzzles, Pauling was able to evaluate the structure of the alpha helix of globular proteins. Pauling then discovered the hydrogen bond that forms between the hydrogen in the amine group of one amino acid and the oxygen from the carboxyl group of another amino acid. The considerable number of hydrogen bonds within a protein that is formed between each amino acid strengthens proteins, (H. Hart, Craine, D.
Hart, 1999). Because of the size of the amino acids and the proteins, the molecule forms a helix. The images below illustrate intramolecular hydrogen bonds.