Protein measurements in the cell

January 28, 2014

A network of chemists at the University of Konstanz has developed an innovative method to study protein structures by means of magnetic labels. The ingenious thing about it is that the magnetic labels are directly incorporated inside the cell when the protein is naturally biosynthesized. The research results, that might have an impact on many areas of structural biology, have been published in the current issue of the renowned Journal of the American Chemical Society.

"Unnatural amino acids with special chemical or biophysical functions that are directly incorporated into proteins in the cell have been known for years. However, despite all efforts it has been impossible so far to develop a magnetic unnatural amino acid. Now we have achieved a real breakthrough," says the Konstanz-based chemist Dr. Daniel Summerer about the research project, which has been conducted in collaboration with the working group of the physical chemist Dr. Malte Drescher from Konstanz. "This has brought us a significant step closer to the final objective of measuring the structure and dynamics of proteins directly in the cell with high precision," Summerer explains.

Proteins that have been modified with the unnatural amino acids from Konstanz can be measured by means of electron paramagnetic resonance spectroscopy (EPR-spectroscopy). Interacting magnetic labels are introduced into strategically selected protein sites. "Measuring the strength of the magnetic interaction enables us to deduce the distance," explains Malte Drescher. "The structure of the protein can be determined by measuring several distances on the nanometer-scale."

In further steps, the scientists intend to implement their method, for which they have filed a patent, for the study of structures in cells: "Our vision is that we will use our method to investigate biologically relevant systems that play a role in e.g. the Parkinson's disease or in regulating the expression of disease-relevant genes", Malte Drescher provides an outlook for the continuation of the research works.

The research was carried out in close collaboration with the Konstanz Research School Chemical Biology. "I am particularly pleased that with this success the valuable work of our two doctoral students, Moritz Schmidt and Julia Borbas, is recognized," says Summerer. For Moritz Schmidt, who has begun his doctoral programme as a Hoechst scholarship holder of the Aventis Foundation less than two years ago, this study is already the second publication as lead author in a particularly prestigious chemical journal.

Explore further: Chemists create protein structure database

More information: M. J. Schmidt, J. Borbas, M. Drescher and D. Summerer. "A genetically encoded spin label for EPR distance measurements." J. Am. Chem. Soc., 2014, DOI: 10.1021/ja411535q.

Related Stories

Chemists create protein structure database

September 9, 2009

(PhysOrg.com) -- Any chemist with access to the Internet can now use a powerful tool to help them accurately identify the structure of a protein, thanks to recently published work led by Harold A. Scheraga, Cornell's Todd ...

A new tool to reveal structure of proteins

March 19, 2012

A new method to reveal the structure of proteins could help researchers understand biological molecules – both those involved in causing disease and those performing critical functions in healthy cells.

Researchers use cells to expand nature's repertoire

December 17, 2013

Using a cell's own internal machinery, Yale researchers have produced proteins not found in nature that can cause cancer in mice, they report Dec. 16 in the Proceedings of the National Academy of Sciences.

Recommended for you

Findings illuminate animal evolution in protein function

July 27, 2015

Virginia Commonwealth University and University of Richmond researchers recently teamed up to explore the inner workings of cells and shed light on the 400–600 million years of evolution between humans and early animals ...

New polymer able to store energy at higher temperatures

July 30, 2015

(Phys.org)—A team of researchers at the Pennsylvania State University has created a new polymer that is able to store energy at higher temperatures than conventional polymers without breaking down. In their paper published ...

How to look for a few good catalysts

July 30, 2015

Two key physical phenomena take place at the surfaces of materials: catalysis and wetting. A catalyst enhances the rate of chemical reactions; wetting refers to how liquids spread across a surface.

Yarn from slaughterhouse waste

July 29, 2015

ETH researchers have developed a yarn from ordinary gelatine that has good qualities similar to those of merino wool fibers. Now they are working on making the yarn even more water resistant.

0 comments

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.