Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Water Is 'Designer Fluid' That Helps Proteins Change Shape

07.08.2008
According to new research, old ideas about water behavior are all wet.

Ubiquitous on Earth, water also has been found in comets, on Mars and in molecular clouds in interstellar space. Now, scientists say this common fluid is not as well understood as we thought.

“Water, as we know it, does not exist within our bodies,” said Martin Gruebele, a William H. and Janet Lycan Professor of Chemistry at the University of Illinois. “Water in our bodies has different physical properties from ordinary bulk water, because of the presence of proteins and other biomolecules. Proteins change the properties of water to perform particular tasks in different parts of our cells.”

Consisting of two hydrogen atoms and one oxygen atom, water molecules are by far the body’s largest component, constituting about 75 percent of body volume. When bound to proteins, water molecules participate in a carefully choreographed ballet that permits the proteins to fold into their functional, native states. This delicate dance is essential to life.

“While it is well known that water plays an important role in the folding process, we usually only look at the motion of the protein,” said Gruebele, who also is the director of the U. of I.’s Center for Biophysics and Computational Biology, and a researcher at the Beckman Institute. “This is the first time we’ve been able to look at the motion of water molecules during the folding process.”

Using a technique called terahertz absorption spectroscopy, Gruebele and his collaborator Martina Havenith at the Ruhr-University Bochum studied the motions of a protein on a picosecond time scale (a picosecond is 1 trillionth of a second).

The technique, which uses ultrashort laser pulses, also allowed the researchers to study the motions of nearby water molecules as the protein folded into its native state.

The researchers present their findings in a paper published July 23 in the online version of the chemistry journal Angewandte Chemie.

Terahertz spectroscopy provides a window on protein-water rearrangements during the folding process, such as breaking protein-water-hydrogen bonds and replacing them with protein-protein-hydrogen bonds, Gruebele said. The remaking of hydrogen bonds helps organize the structure of a protein.

In tests on ubiquitin, a common protein in cells, the researchers found that water molecules bound to the protein changed to a native-type arrangement much faster than the protein. The water motion helped establish the correct configuration, making it much easier for the protein to fold.

“Water can be viewed as a ‘designer fluid’ in living cells,” Gruebele said. “Our experiments showed that the volume of active water was about the same size as that of the protein.”

The diameter of a single water molecule is about 3 angstroms (an angstrom is about one hundred-millionth of a centimeter), while that of a typical protein is about 30 angstroms. Although the average protein has only 10 times the diameter of a water molecule, it has 1,000 times the volume. Larger proteins can have hundreds of thousands times the volume. A single protein can therefore affect, and be influenced by, thousands of water molecules.

“We previously thought proteins would affect only those water molecules directly stuck to them,” Gruebele said. “Now we know proteins will affect a volume of water comparable to their own. That’s pretty amazing.”

With Gruebele and Havenith, co-authors of the paper are graduate student Seung Joong Kim at the U. of I., and graduate student Benjamin Born at the Ruhr-University Bochum.

Funding was provided by the Human Frontier Science Program and the National Science Foundation.

James E. Kloeppel | University of Illinois
Further information:
http://www.illinois.edu

Further reports about: Computational Biology Gruebele angstrom water molecules

More articles from Life Sciences:

nachricht Ion treatments for cardiac arrhythmia — Non-invasive alternative to catheter-based surgery
20.01.2017 | GSI Helmholtzzentrum für Schwerionenforschung GmbH

nachricht Seeking structure with metagenome sequences
20.01.2017 | DOE/Joint Genome Institute

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Traffic jam in empty space

New success for Konstanz physicists in studying the quantum vacuum

An important step towards a completely new experimental access to quantum physics has been made at University of Konstanz. The team of scientists headed by...

Im Focus: How gut bacteria can make us ill

HZI researchers decipher infection mechanisms of Yersinia and immune responses of the host

Yersiniae cause severe intestinal infections. Studies using Yersinia pseudotuberculosis as a model organism aim to elucidate the infection mechanisms of these...

Im Focus: Interfacial Superconductivity: Magnetic and superconducting order revealed simultaneously

Researchers from the University of Hamburg in Germany, in collaboration with colleagues from the University of Aarhus in Denmark, have synthesized a new superconducting material by growing a few layers of an antiferromagnetic transition-metal chalcogenide on a bismuth-based topological insulator, both being non-superconducting materials.

While superconductivity and magnetism are generally believed to be mutually exclusive, surprisingly, in this new material, superconducting correlations...

Im Focus: Studying fundamental particles in materials

Laser-driving of semimetals allows creating novel quasiparticle states within condensed matter systems and switching between different states on ultrafast time scales

Studying properties of fundamental particles in condensed matter systems is a promising approach to quantum field theory. Quasiparticles offer the opportunity...

Im Focus: Designing Architecture with Solar Building Envelopes

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...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Sustainable Water use in Agriculture in Eastern Europe and Central Asia

19.01.2017 | Event News

12V, 48V, high-voltage – trends in E/E automotive architecture

10.01.2017 | Event News

2nd Conference on Non-Textual Information on 10 and 11 May 2017 in Hannover

09.01.2017 | Event News

 
Latest News

Helmholtz International Fellow Award for Sarah Amalia Teichmann

20.01.2017 | Awards Funding

An innovative high-performance material: biofibers made from green lacewing silk

20.01.2017 | Materials Sciences

Ion treatments for cardiac arrhythmia — Non-invasive alternative to catheter-based surgery

20.01.2017 | Life Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>