High-speed atomic force microscopy takes on intrinsically disordered proteins

KANAZAWA, Japan, Dec. 4, 2020 /PRNewswire/ — Kanazawa University’s pioneering high-speed atomic force microscope technology has now shed light on the structure and dynamics of some of life’s most ubiquitous and inscrutable molecules – intrinsically disordered proteins. The study is reported in Nature Nanotechnology.

Our understanding of biological proteins does not always correlate with how common or important they are. Half of all proteins, molecules that play an integral role in cell processes, are intrinsically disordered, which means many of the standard techniques for probing biomolecules don’t work on them. Now researchers at Kanazawa University in Japan have shown that their home-grown high-speed atomic force microscopy technology can provide information not just on the structures of these proteins but also their dynamics.

Understanding how a protein is put together provides valuable clues to its functions. The development of protein crystallography in the 1930s and 1950s brought several protein

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Folding proteins feel the heat, and cold

Folding proteins feel the heat, and cold
An illustration shows the dynamics of protein folding in a solution as previously understood and as revealed by new models developed at Rice University, Tulane University and the Johns Hopkins University School of Medicine. Credit: Dilip Asthagiri

It’s a long-standing assumption that the presence of water influences how proteins fold. A new study is challenging the details.

A paper in the American Chemical Society’s Journal of Physical Chemistry Letters shows proteins that presumably evolved to avoid water as they fold may actually behave in ways scientists did not anticipate.

That discovery could change how scientists think about hydrophobic (water-avoiding) and hydrophilic (water-attracting) interactions in solutions, according to a Rice University engineer.

Collaborators from Rice and Tulane universities and the Johns Hopkins University School of Medicine created atom-level models of polypeptides that showed folding is also influenced by thermal expansion of the solvents they occupy, but not in ways that match

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Microscopy breakthrough reveals how proteins behave in 3-D

Microscopy breakthrough reveals how proteins behave in 3D
A new microscopy system that can can image individual molecules in 3D and capture the way they “wobble” uses a specially engineered glass plate developed by University of Rochester optical scientists. Credit: University of Rochester photo / J. Adam Fenster

Six years ago, the Nobel Prize in chemistry was awarded to three scientists for finding ways to visualize the pathways of individual molecules inside living cells.

Now, researchers at the University of Rochester and the Fresnel Institute in France have found a way to visualize those molecules in even greater detail, showing their position and orientation in 3-D, and even how they wobble and oscillate. The work could shed invaluable insights into the biological processes involved, for example, when a cell and the proteins that regulate its functions react to the virus that causes COVID-19.

“When a protein changes shape, it exposes other atoms that enhance the biological process, so

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