In his father's house Paul Boyer marries Lyda Whicker. Together they move to Madison.
Boyer enters Brigham Young University where he earns his BS in chemistry. He attends with interest a course in qualitative and quantitative analysis by John Wing, who instils in him appreciation for accurate measurement. Boyer’s enthusiasm for general chemistry is due to Joe Nichol, passion for organic chemistry to Charles Maw. Uncertain about his future, Boyer submits an application for a Wisconsin Alumni Research Foundation (WARF) Scholarship for graduate studies. The answer is positive.
Boyer is Founding Director of the Molecular Biology Institute. He formulates three postulates for the binding mechanism for ATP synthesis.
Paul Boyer spends with his family a memorable summer at the Woods Hole Marine Biological Laboratories on Cape Cod.
Boyer's group finds the first postulate: energy input is not used primarily to form the ATP molecule, but to promote the release of an already formed and tightly bound ATP. In the following decade, other two postulates are formulated: three identical catalytic sites go through compulsory, sequential binding changes; binding changes of the catalytic subunits, circularly arranged on the periphery of the enzyme, are driven by the rotation of an internal subunit.
Paul Boyer accepts an Hill Foundation Professorship at University of Minnesota. His group's research is mostly on enzymes other than the ATP synthase. Much of their effort are directed toward attempting to detect a possible phosphorylated intermediate in ATP (adenosine triphosphate) synthesis using 32P as a probe. They finally discover a new type of phosphorylated protein, a catalytic intermediate in ATP formation with a phosphoryl group attached to a histidine residue.
Paul Boyer enters University of Wisconsin at Madison where he earns his MS in chemistry. Biochemistry Department is at that time focused on the excitement of vitamins, nutrition and metabolism. Researchers test irradiation of milk for enrichment with vitamin D, the potentiality of nicotinic acid to cure pellagra, identification and separation of bacterial growth factors, isolation and identification of vitamin K antagonist and many other topics.
Boyer's local War Draft Board in Provo calls him to become a member of the U.S. Navy. Boyer works in a private laboratory at the Navy Medical Research Institute in Bethesda, Maryland.
Paul Boyer receives one half of the Nobel Prize in Chemistry along with John E. Walker "for their elucidation of the enzymatic mechanism underlying the synthesis of adenosine triphosphate (ATP)".
Paul Boyer attends Provo High School, where he is active in student government and the debating team. He graduates when he is only 16.
Paul Boyer travels to Sweden as Guggenheim Fellow. Here he leads researches at Wenner-Gren Institute of the University of Stockholm with Olov Lindberg and Lars Ernster, and at the Nobel Medical Institute, working with Hugo Theorell's group on the mechanism of alcohol dehydrogenase.
Paul Boyer, together with several graduate students and postdocs, moves to a new wing of the chemistry building at University of California in Los Angeles (UCLA). There they find that the enzyme-bound phosphohistidine is an intermediate in the substrate level phosphorylation of the citric acid cycle.
Paul Boyer is born in Provo, Utah as one of 6 children. His father, Dell Delos Boyer, teaches him logical reasoning, compassion, love of others, honesty, and discipline, but also practical activities as pitching horseshoes and growing vegetables. His mother, Grace Guymont, dies at the age of 45. Her death contributes to Boyer's later interest in studying biochemistry. His first interest for chemistry arises when he receives a chemistry set for Christmas.
Boyer spends war's years at Stanford University on a war-related research project dedicated to stabilization of serum albumin for transfusions, sponsored by the Committee on Medical Research. He works under the direction of J. Murray Luck. The research group discovers that long chain fatty acids remarkably stabilize serum albumin to heat denaturation, and even reverse the denaturation by heat or concentrated urea solutions. Thanks to Stanford years, Boyer gains experience with proteins.
Paul Boyer earns his Ph.D. in Biochemistry at University of Wisconsin. Boyer works with Henry Lardy under Professor Paul Phillips, who encourages them to explore metabolic and enzyme interests. Boyer attends symposiums held by biochemical giants as Otto Meyerhof, Fritz Lipmann, and Carl Cori and he treasures the evening research discussion groups centred on enzymes and metabolism.