No one has ever seen exactly how water molecules interact with proteins – even though water is the essential element for life . . . that is, not until now.
Researchers led by Ohio State University physicist Dongping Zhong revealed these interactions for the first time, and report the results in the current issue of the Proceedings of the National Academy of Sciences.
Proteins are complex molecules that form the main support structure for plant and animal cells, and they also regulate biochemical reactions.
Zhong's project aims eventually to explain how water helps enable life-supporting biological functions such as protein folding or enzyme catalysis. But for now, this early result ends decades of controversy on what happens in the microscopic realm where water and proteins meet.
The controversy, Zhong explained, stemmed from the fact that researchers across different disciplines used different methods to study the problem. Because of that, they got different answers on the speed with which these essential biochemical reactions take place.
"A biologist will tell you that water and proteins must interact on a nanosecond [one billionth of a second] time scale, because that's how fast proteins move," he said. "And a physicist will tell you that the interaction would happen much faster -- on the picosecond [one trillionth of a second] time scale -- because that's how fast water molecules move. And someone who uses X-rays will give you a different answer than someone who uses nuclear magnetic resonance and so on."
"My feeling is that there is no real controversy -- everybody is just looking at the same answer from different angles," he added.
The answer, revealed in Zhong's lab: water molecules do move fast on their own, but they slow down -- to a speed midway between the nanosecond and picosecond scale -- to connect with proteins.
Zhong, an assistant professor of physics, used ultra-fast laser pulses to take snapshots of water molecules moving around a protein taken from a common bacterium, Staphylococcus.
The key to getting a good view of the interaction was to precisely locate an optical probe on the protein surface. They inserted a molecule of the amino acid tryptophan into the protein as a probe, and measured how water moved around it -- a technique Zhong began to develop when he was a postdoctoral researcher in Nobel laureate Ahmed Zewail's lab at the California Institute of Technology 5 years ago.
Laser studies of the protein while it was immersed in water revealed that far away from the protein -- in a region Zhong called "bulk water" -- the water molecules were flowing around each other at their typically fast speeds, with each movement requiring only a single picosecond.
But the water near the protein formed several distinct layers. The outermost layer flowed at a slower speed than in bulk water, and the innermost layer even slower. In that innermost layer, each movement of a water molecule to connect with the protein required at least 100 picoseconds to complete.
So when it comes to supporting life -- on the molecular scale, anyway -- water has to move 100 times slower to get the job done.
"The fast-moving water has to slow down to connect with a slow-moving protein -- it's that simple," Zhong said.
"It sounds trivial, I know. But it should be trivial.
"It's an essential biological interaction that has to work just right every time. If the water moved too slowly, it could get in the way of proteins trying to meet -- it would be a bottleneck in the process. And if it moved too fast, it couldn't connect with the protein at all. So I think this is nature's way of getting the interaction just right."
Zhong and Zewail's coauthors on the paper included Weihong Qiu, Ta-Ting Kao, Luyuan Zhang, Yi Yang, and Lijuan Wang of Ohio State and Wesley E. Stites of the University of Arkansas . Zhong is now working with Ohio State chemist Sherwin Singer to create computer simulations of protein-water motions based on these results. That work is being done at the Ohio Supercomputer Center.
This work was supported by the Petroleum Research Fund, the Packard Foundation, the National Science Foundation, and the National Institutes of Health.
Dongping Zhong | EurekAlert!
Nanoparticle Exposure Can Awaken Dormant Viruses in the Lungs
16.01.2017 | Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt
Cholera bacteria infect more effectively with a simple twist of shape
13.01.2017 | Princeton University
Among the general public, solar thermal energy is currently associated with dark blue, rectangular collectors on building roofs. Technologies are needed for aesthetically high quality architecture which offer the architect more room for manoeuvre when it comes to low- and plus-energy buildings. With the “ArKol” project, researchers at Fraunhofer ISE together with partners are currently developing two façade collectors for solar thermal energy generation, which permit a high degree of design flexibility: a strip collector for opaque façade sections and a solar thermal blind for transparent sections. The current state of the two developments will be presented at the BAU 2017 trade fair.
As part of the “ArKol – development of architecturally highly integrated façade collectors with heat pipes” project, Fraunhofer ISE together with its partners...
At TU Wien, an alternative for resource intensive formwork for the construction of concrete domes was developed. It is now used in a test dome for the Austrian Federal Railways Infrastructure (ÖBB Infrastruktur).
Concrete shells are efficient structures, but not very resource efficient. The formwork for the construction of concrete domes alone requires a high amount of...
Many pathogens use certain sugar compounds from their host to help conceal themselves against the immune system. Scientists at the University of Bonn have now, in cooperation with researchers at the University of York in the United Kingdom, analyzed the dynamics of a bacterial molecule that is involved in this process. They demonstrate that the protein grabs onto the sugar molecule with a Pac Man-like chewing motion and holds it until it can be used. Their results could help design therapeutics that could make the protein poorer at grabbing and holding and hence compromise the pathogen in the host. The study has now been published in “Biophysical Journal”.
The cells of the mouth, nose and intestinal mucosa produce large quantities of a chemical called sialic acid. Many bacteria possess a special transport system...
UMD, NOAA collaboration demonstrates suitability of in-orbit datasets for weather satellite calibration
"Traffic and weather, together on the hour!" blasts your local radio station, while your smartphone knows the weather halfway across the world. A network of...
Fiber-reinforced plastics (FRP) are frequently used in the aeronautic and automobile industry. However, the repair of workpieces made of these composite materials is often less profitable than exchanging the part. In order to increase the lifetime of FRP parts and to make them more eco-efficient, the Laser Zentrum Hannover e.V. (LZH) and the Apodius GmbH want to combine a new measuring device for fiber layer orientation with an innovative laser-based repair process.
Defects in FRP pieces may be production or operation-related. Whether or not repair is cost-effective depends on the geometry of the defective area, the tools...
10.01.2017 | Event News
09.01.2017 | Event News
05.01.2017 | Event News
16.01.2017 | Power and Electrical Engineering
16.01.2017 | Information Technology
16.01.2017 | Power and Electrical Engineering