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| Milton Harris: A Biography |
| by Jon H. Georg. 1998 |
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In 1924, at the age of sixteen, Harris began his college education at Oregon State University, then known as Oregon Agricultural
College. During his three years at Oregon Agricultural College, Milton Harris was involved with a wide variety of programs
on campus. These included: Phi Sigma Kappa, Freshman Tennis, Varsity Tennis, Interclass Basketball, the Circle "O" Association,
Chi Epsilon (Local Honorary in Chemistry), and Tau Beta Pi (National Honorary in Engineering). Despite the lack of a chemistry
department at that time, Harris pursued a degree in Chemical Engineering and took all of the available courses in chemistry.
While a sophomore, Harris was called in to meet with his advisor, who told him that he had taken more chemistry courses than
anyone at the University and that he was almost done with his course work. His advisor then told him about a twelve-week course
in chemistry at the University of Washington that would allow him to graduate early. This advisor asked about Harris' future
plans, to which Harris said that he would probably get a job, and that the only job he was aware of was an analytical chemist
position in Portland at the gas company. His advisor told him that furthering his education by going to graduate school would
probably be a good idea. Harris responded with a question: "What's a graduate school?"
It was at the NBS that Milton Harris, along with Vincent duVigneaud, made his first big discovery. The men observed similarities
between the three-dimensional molecular structures of wool, insulin, and human hair. They realized that all of these three-dimensional
polymers are held together by cystine disulfide linkages. The hormone insulin is a protein with covalently connects polypeptide
chains. Disulfide bonds holding these chains together with noncovalent forces are easily separable, and cystine is the product
of oxidation between pairs of cysteine side chains that form a disulfide bond. The presence of these disulfide bonds in cystine
proteins often plays an important structural role. Disulfide bonds, while relatively rare, are found primarily in proteins
exported from cells. When disulfide bonds are reduced the protein unfolds, but upon reoxidation these disulfide bonds are
reformed, which is an unexpected reformation. In the reoxidation, cysteine bonds are formed, which, given time, oxidize into
the disulfide bonds in a cystine protein, thus providing a more stable structure. Hair consists of a fibrous protein called
keratin, which contains an unusually large number of disulfide bonds. To straighten or curl hair, a reducing agent is used,
which temporarily dissolves the disulfide bonds. After the hair has been curled or straightened, an oxidizing agent is used
to reform the disulfide bonds. Since these disulfide bonds are no longer in their original position, the hair holds its new
shape.
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