Dr. Herbert A. Hauptman | WNY Scientist 2007

Herbert-HauptmanNobel Laureate Herbert A. Hauptman, Ph.D., has been recognized by the highest levels of academia, the international science community, and the media because his work in the fields of mathematics and science saves lives. The Buffalo News said that because of his lifelong dedication to molecular level research “Hauptman…Undoubtedly saved more lives…than anyone else in recent history.” Through his work at the Hauptman-Woodward Medical Research Institute, Dr. Hauptman continues to pave the way for pharmaceutical breakthroughs, advances in medical procedures, and the groundbreaking research done by his fellow crystallographers throughout the world.

Born in New York City in 1917, Dr. Hauptman received his bachelor’s degree from City College in 1937, his master’s degree from Columbia in 1939, and his doctoral degree from the University of Maryland in 1955.

About the work which led to Dr. Herbert A. Hauptman’s 1985 Nobel Prize in Chemistry

When a beam of x-rays strikes a crystal, the incident beam is split into many weaker beams having different directions and different intensities, thus giving rise to what’s called the diffraction pattern. The nature of the diffraction pattern, which is to say the directions and intensities of the scattered x-rays, is determined by the structure of the crystal, that is the arrangement of the atoms in the crystal.

If one knew the structure of the crystal, one could readily predict the nature of the diffraction pattern, that is the directions and intensities of the x-rays scattered by the crystal.

However, the problem facing the crystallographer is the converse: One observes the diffraction pattern – that is one measures the directions and intensities of the X-Rays scattered by the crystal. Can one then deduce the structure of the crystal, that is the atomic arrangement, giving rise to the observed diffraction pattern?

The 1985 Nobel Prize in Chemistry was given for the solution of this problem.

The ability to solve crystal structures rapidly and routinely had important consequences. Possibly the most important was the ability to relate crystal and molecular structures to biological activity. Thus it became possible to understand life processes at the “molecular” level, to understand better how living things “work,” and the cause of disease, and to devise better therapies and better drugs for the prevention and treatment of disease with a minimum of adverse side effects, in short to improve human health.

X-rays strike a crystal. The crystal contains a molecule, which is repeated throughout the whole crystal in all directions. The crystal deflects the x-rays in certain definite directions so that the radiation can be seen as spots of different intensity such as in a photographic film.