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Nobel Winner Huber Explores Proteins

News Feature

By Kris J. Thiessen

A full house gathered in Science Center D yesterday afternoon to hear Nobel prize-winner Robert Huber speak about his research in determining molecular structures.

Huber, who was awarded the 1988 Nobel prize in Chemistry, is the director of the Max-Planck-Institut fur Biochemie in Martinsried, Germany.

Huber's speech, "Structure and Function of Large Proteins and Protein Assemblies by X-Ray Crystallography and Electron Microscopy," was the 1997 Max Tishler Prize Lecture, established in 1951 by an award from the Merck Sharp & Dohme Company.

Huber's research is two-fold: it focuses both on the structure and function of biological macro-molecules and on their functional importance. Additionally, he studies experimental methods for the X-ray crystallography of proteins.

Proteins are the basic machinery of cells--they are responsible for every process that occurs in the body. X-ray crystallography is a technique used for mapping a protein's structure atom-by-atom to create a three-dimensional model, much like a fingerprint.

"Without structure, there is no biochemistry and no biology," Huber said. "I think that [structural biology] is the field in science that offers adventure more than any other because each of these large proteins that we look at is for me like discovering a new island."

Huber said that despite scientists' knowledge of the environments in which we live, the basic processes of life are not as well understood.

"There are no new unknown islands to be discovered nowadays: we know every centimeter of the earth from satellites, but [proteins] are the new islands to be discovered," he said. "That is one point that is a great draw for me personally."

Huber stressed the importance of using the structures of proteins to determine their function in cellular processes.

"How should we understand the biology [and] the biochemistry without knowing the structure of the molecules that carry out those jobs that form cellular aggregates that carry out the enzymatic functions?" Huber asked.

Huber said that because proteins are the basis for everything that happens in the body, they are central to biology.

"If you look at modern biochemistry textbooks, there is a transformation," Huber said. "[Today], you find pictures of proteins on every page, while ten years ago, there were only a few hemoglobin structures."

Huber cites the proliferation of structural information in basic texts as proof of its centrality in modern biochemistry.

"There is [now] an appreciation of the importance of structural information for our understanding of biochemistry and biology," he said.

Huber noted that many of the examples he presented are targets of pharmaceutical drug design, one of the interests of Max Tishler.

"[The clinical significance is] the implication of the structures for drug design, drug discovery and drug development," Huber said.

Huber began his lecture by describing how structural biology could be used to view organisms as a sum of their parts.

"I [present] the nightmare of a structural biologist--to see a mouse at atomic resolution," Huber said. This task is analogous to finding a needle in a hay stack.

Diagramming the method for separating a mouse into its components, Huber suggested the use of tomography, electron microscopy, biochemical analysis, crystal decoration, X-ray crystallography and nuclear magnetic resonance (NMR) imaging for high-resolution, atomic detail.

Huber described the work his research group has done with several protein structures, emphasizing the complementarity of relatively low-resolution electron microscopy and high-resolution X-ray crystallography.

"Electron microscopy helps to overcome the phase problem [of crystallography], providing the initial picture that is sufficient for carrying out the [X-ray] high resolution studies," Huber said.

In addition to developing new drugs, Huber said this type of work is of interest to the average person.

"For the person on the street, I think yes, [they] would like to know how nature's bodies function [and] how their bodies function," Huber said. "It is on our side to make our research understandable, and the better it is for us all."

Huber said the development of his interest in structural biology is an adventure.

"I studied chemistry, and realized that crystal structures had a particular appeal for me," Huber said.

Huber said he started his research by examining small molecule crystal structures.

"I started to like the method of crystallography and the results, the precise atomic arrangements of large molecules," Huber said. "I thought the field was packed with this discovery aspect, which I was interested by."

Huber will deliver a second lecture, "Proteolytic Enzymes and Their Inhibitors, Structures, Functions and Tools for Basic Science and Medicine," today at 5 p.m. in the Pfizer Lecture Hall, Mallinckrodt MB-23. Both lectures are sponsored by the Department of Chemistry and Chemical Biology.CrimsonKris J. TheissenGREGORY L. VERDINE presents ROBERT HUBER with the 1997 Max Tishler Prize Lecturer Award.

"I [present] the nightmare of a structural biologist--to see a mouse at atomic resolution," Huber said. This task is analogous to finding a needle in a hay stack.

Diagramming the method for separating a mouse into its components, Huber suggested the use of tomography, electron microscopy, biochemical analysis, crystal decoration, X-ray crystallography and nuclear magnetic resonance (NMR) imaging for high-resolution, atomic detail.

Huber described the work his research group has done with several protein structures, emphasizing the complementarity of relatively low-resolution electron microscopy and high-resolution X-ray crystallography.

"Electron microscopy helps to overcome the phase problem [of crystallography], providing the initial picture that is sufficient for carrying out the [X-ray] high resolution studies," Huber said.

In addition to developing new drugs, Huber said this type of work is of interest to the average person.

"For the person on the street, I think yes, [they] would like to know how nature's bodies function [and] how their bodies function," Huber said. "It is on our side to make our research understandable, and the better it is for us all."

Huber said the development of his interest in structural biology is an adventure.

"I studied chemistry, and realized that crystal structures had a particular appeal for me," Huber said.

Huber said he started his research by examining small molecule crystal structures.

"I started to like the method of crystallography and the results, the precise atomic arrangements of large molecules," Huber said. "I thought the field was packed with this discovery aspect, which I was interested by."

Huber will deliver a second lecture, "Proteolytic Enzymes and Their Inhibitors, Structures, Functions and Tools for Basic Science and Medicine," today at 5 p.m. in the Pfizer Lecture Hall, Mallinckrodt MB-23. Both lectures are sponsored by the Department of Chemistry and Chemical Biology.CrimsonKris J. TheissenGREGORY L. VERDINE presents ROBERT HUBER with the 1997 Max Tishler Prize Lecturer Award.

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