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Chemistry faculty can relate to Nobel Prize-winning microscopy research


MONMOUTH, Ill. – Monmouth College chemistry professors were excited to learn that the 2017 Nobel Prize in Chemistry went Oct. 4 to scientists working with cryo-electron microscopy.

The Nobel Prize committee said that work by scientists Jacques Dubochet, Joachim Frank and Richard Henderson has “moved biochemistry into a new era,” and Monmouth professors say there’s no telling how mainstream it will become in the next few years.

Cryo-electron microscopy has only recently become useful as a technique for biological molecules because of new detector technology that has been developed in the past few years, according to Monmouth chemistry professor Laura Moore.

Previously, scientists had two options for analyzing biological structures at high (near atomic) resolution: X-ray crystallography or nuclear magnetic resonance spectroscopy (NMR). Today, in the main repository of biological molecular structures (the Protein Databank), there are about 120,000 structures solved by X-ray crystallography; 12,000 solved by NMR; and less than 2,000 solved by electron microscopy.

“I would guess that the number of structures solved by electron microscopy will increase rapidly,” said Moore. “In the labs here at Monmouth, we do use microscopy techniques such as atomic force microscopy, and we have even used them to investigate biological molecules and interactions of biological molecules. However, the experiments we do aren’t anywhere near the resolution of cryo-electron microscopy. It will be interesting to see how this technique becomes more widely used in the next few years.”

One of Moore’s department colleagues, Audra Sostarecz, works with imaging techniques in several activities, including teaching “Instrumental Analysis” at Monmouth and as a mentor to a research group that analyzes biomolecules at the small scale. Sostarecz earned a doctorate from Penn State University, which has an imaging mass spectrometry lab.

“I am always excited to discuss imaging techniques with students,” said Sostarecz. “Every year, we talk about the 1986 Nobel Prize in Physics for the development of scanning tunneling microscopy. Along with this, I use the atomic force microscope in my research group here, as well as scanning electron microscopy. I am thrilled that in a few short months, I will be discussing this newest Nobel Prize in Chemistry with my students and that it will be one more advantage to using imaging techniques to study biological samples.”

Moore said the work by the Nobel Prize-winning scientists may impact many areas, including her own research.

“For X-ray crystallography, crystals of the biological molecules need to be grown and some are extremely difficult to crystallize,” said Moore. “The protein I've worked on for 20 years still does not have structure because it won’t crystallize. NMR spectroscopy has a size limitation for the molecule and also requires highly concentrated solutions, so it is not possible to obtain a structure for large biological molecules or complexes of biological molecules.”

Cryo-electron microscopy eliminates both the need for crystals and does not have the size limitation of NMR, she said.

“This microscopy technique also produces structures that are a better representation of what these biomolecules look like in nature (because the molecules are frozen in a native environment) than the structures that come from an ordered crystal or a highly concentrated solution,” said Moore. “So these microscopy structures may be more useful for designing drugs that bind to specific proteins or for understanding how biological molecules interact.”