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!
World’s Largest Study on Allergic Rhinitis Reveals new Risk Genes
17.07.2018 | Helmholtz Zentrum München - Deutsches Forschungszentrum für Gesundheit und Umwelt
Plant mothers talk to their embryos via the hormone auxin
17.07.2018 | Institute of Science and Technology Austria
For the first time ever, scientists have determined the cosmic origin of highest-energy neutrinos. A research group led by IceCube scientist Elisa Resconi, spokesperson of the Collaborative Research Center SFB1258 at the Technical University of Munich (TUM), provides an important piece of evidence that the particles detected by the IceCube neutrino telescope at the South Pole originate from a galaxy four billion light-years away from Earth.
To rule out other origins with certainty, the team led by neutrino physicist Elisa Resconi from the Technical University of Munich and multi-wavelength...
For the first time a team of researchers have discovered two different phases of magnetic skyrmions in a single material. Physicists of the Technical Universities of Munich and Dresden and the University of Cologne can now better study and understand the properties of these magnetic structures, which are important for both basic research and applications.
Whirlpools are an everyday experience in a bath tub: When the water is drained a circular vortex is formed. Typically, such whirls are rather stable. Similar...
Physicists working with Roland Wester at the University of Innsbruck have investigated if and how chemical reactions can be influenced by targeted vibrational excitation of the reactants. They were able to demonstrate that excitation with a laser beam does not affect the efficiency of a chemical exchange reaction and that the excited molecular group acts only as a spectator in the reaction.
A frequently used reaction in organic chemistry is nucleophilic substitution. It plays, for example, an important role in in the synthesis of new chemical...
Optical spectroscopy allows investigating the energy structure and dynamic properties of complex quantum systems. Researchers from the University of Würzburg present two new approaches of coherent two-dimensional spectroscopy.
"Put an excitation into the system and observe how it evolves." According to physicist Professor Tobias Brixner, this is the credo of optical spectroscopy....
Ultra-short, high-intensity X-ray flashes open the door to the foundations of chemical reactions. Free-electron lasers generate these kinds of pulses, but there is a catch: the pulses vary in duration and energy. An international research team has now presented a solution: Using a ring of 16 detectors and a circularly polarized laser beam, they can determine both factors with attosecond accuracy.
Free-electron lasers (FELs) generate extremely short and intense X-ray flashes. Researchers can use these flashes to resolve structures with diameters on the...
13.07.2018 | Event News
12.07.2018 | Event News
03.07.2018 | Event News
17.07.2018 | Information Technology
17.07.2018 | Materials Sciences
17.07.2018 | Power and Electrical Engineering