U.S., German Scientists Win Nobel Prizes

Three American researchers, including one from California, were awarded the 1988 Nobel Prize for Physics on Wednesday for their research on an infinitesimal, ghostlike particle called the neutrino.

Their research led to a better understanding of the so-called “weak force” that holds atoms together and “opened entirely new opportunities for research into the innermost structure and dynamics of matter,” the Nobel citation said.

The award, announced by the Royal Swedish Academy of Sciences in Stockholm, ended a five-year drought during which no Americans had won the prestigious physics prize.

Structure of Key Proteins

Also on Wednesday, the academy announced that three West Germans would share the Nobel Prize for Chemistry for their work in using X-rays to determine the structure of key proteins in the photosynthetic process by which plants convert sunlight into sugars that can be used by plant cells.

The 1988 award marked the second time in four years that the chemistry Nobel was presented for such X-ray crystallographic studies, indicating the great importance that scientists are placing on identifying the precise three-dimensional structures of molecules that are important in biological processes.

The physics award was shared by: Melvin Schwartz, 55, a former Stanford University professor who is now president of his own computer company, Digital Pathways of Mountain View; Leon Lederman, 66, director of the Fermi National Accelerator Laboratory in Batavia, Ill., and Jack Steinberger, 67, a German-born naturalized American who is now working at the Center for European Nuclear Research in Geneva, Switzerland.

The chemistry prize was awarded to: Hartmut Michel, 40, of the Max Planck Institute for Biophysics in Frankfurt; Robert Huber, 51, of the Max Planck Institute for Biochemistry in Martinsried, and Johann Diesenhofer, 45, a West German who is now at the Howard Hughes Medical Institute in Dallas.

The two awards displayed a marked difference in timeliness, with the physics prize being awarded for “an experiment that was completed and published in 1961,” Lederman said at a news conference Wednesday. “Those poor guys in Stockholm have been puzzling over it ever since and finally decided it was good stuff.”

In contrast, the chemistry prize was for work completed only three years ago.

Conceived at Coffee Breaks

The three physicists conceived their ground-breaking work during coffee breaks while all were working at Columbia University during the late 1950s. They reasoned that the weak force could be examined with a beam of subatomic particles but concluded that simple protons, neutrons or electrons would not give the desired information.

The little-understood neutrino would, but its use presented formidable obstacles. They would have to find a way to produce and focus a beam of the particles, which have no electrical charge and, even in comparison to protons and electrons, negligible mass.

They also would have to detect the motion of neutrinos after the beam had interacted with target atoms; that motion would reveal important new details about atomic structure and the nature of the weak force. But neutrino detectors did not exist, so they had to invent one.

Over a two-year period, the three achieved both objectives and, in the process, transformed “the ghostly neutrino into an active tool of research,” the Nobel citation said. They also discovered that there are two different types of neutrinos, one linked to electrons and one linked to another type of particle called a muon.

‘All Over the Place’

“We started a sort of cottage industry in identifying basic particles, the quarks and so on,” Lederman said. “Now there are hot- and cold-running neutrinos all over the place.”

In his own news conference, Schwartz said their discovery had “no practical significance.” But “if you understand something better, sooner or later it will be practical,” he added.

Like his colleagues, Schwartz said he had given up on receiving the Nobel. “I thought of it (the Nobel) in the 1960s, and I thought a lot less of it in the 1970s, and not at all in the 1980s. . . . But I was pretty well known (among his colleagues) for what I did back in (1961). It didn’t matter to me if I had a prize or no prize.”

Lederman noted that he hopes the award will help persuade the federal government to fund the proposed superconducting supercollider, which would be used to search for other subatomic particles.

The chemistry award, meanwhile, was given for two reasons, according to the academy: the development of a new technique and its use to study an important molecule. The three West German researchers were the first to succeed in unraveling the structural details of a membrane-bound protein.

Most of the proteins that regulate a cell’s interaction with its environment are located in the cellular membrane, including receptors for drugs, hormones and nerve impulses and proteins that transport nutrients into the cell.

‘Important Class of Molecules’

“These are an important class of molecules for which there is very little information,” biochemist Douglas Rees of UCLA said. By determining the structure of one protein in the membrane, the West German researchers produced insights into the nature of all the membrane-bound proteins and showed how their properties could be determined.

Furthermore, the particular protein whose structure the three determined, the “photosynthetic reaction center,” controls what the Nobel citation called “the most important chemical reaction on Earth. . . . All our nourishment has its origin in this process, which is called photosynthesis and which is a condition for all life on Earth.”

To use X-rays to determine the structure of a protein, it is necessary to obtain the protein in a crystalline form in which the individual protein molecules are arrayed in a highly regular manner. Such crystals are generally produced by precipitating the proteins from water, in much the same fashion that sugar crystals are formed when a hot, concentrated solution of sugar is cooled.

Won’t Naturally Dissolve

Producing crystals from proteins found in the interior of cells is difficult. Producing them from membrane proteins was impossible until Michel developed a technique to do so in 1982. The problem was that these proteins, which normally exist in the oily interior of membranes, will not naturally dissolve in water and thus cannot be crystallized. Michel devised a technique for dissolving them that used detergents and certain other chemicals.

“Thanks to the method of crystallization developed by Hartmut Michel, the prospects of obtaining detailed structural information for other membrane proteins have improved,” according to the Nobel citation.

Times staff writer Mark A. Stein, in San Francisco, contributed to this story.