Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

How the “Biological Spark Plug” in Biomolecular Motors Works

04.08.2014

Heidelberg researchers simulate processes that trigger muscle movement

Using high-performance computers and quantum mechanical methods, researchers at Heidelberg University have simulated processes that reveal how the “biological spark plug” works in the biomolecular motors of cells. Under the direction of Dr. Stefan Fischer, the investigations focused on the myosin protein, which, among other things, is responsible for muscle movement.

The researchers’ extensive simulations show how the release of energy is initiated in this complex motor. The results of the research conducted at the Interdisciplinary Center for Scientific Computing were published in the journal PNAS.

Biomolecular motors are protein molecules responsible for mechanical movement in cells. These smallest of known motors use the molecule adenosine triphosphate (ATP) as fuel, which all living organisms use as a source of energy for processes that require it. In order to understand how these cell motors use ATP to function, they can be compared to an automobile engine, in which energy is released by burning petrol.

Because petrol does not ignite by itself, energy must be applied to initiate the combustion reaction. This job is done by the spark plug. Energy is not released until the heat energy of the spark is applied to overcome the energy barrier of petrol combustion. According to Stefan Fischer, there are a number of parallels to biomolecular motors. The ATP molecule is stable and like petrol does not release its energy spontaneously. Whereas ATP splits rather than burns, there is also an energy barrier that must be crossed to trigger that splitting, known as hydrolysis.

Dr. Fischer’s research team studied exactly how the trigger mechanism for energy release works in biomolecular motors. “We wanted to find out how the energy stored in the ATP gets released so selectively and precisely timed,” explains the Heidelberg researcher, who heads the Biological Macromolecules working group at the Interdisciplinary Center for Scientific Computing (IWR).

The scientists launched their study of the “biological spark plug” using the biomolecular motor myosin. Myosin is a family of motor proteins that uses ATP, for example to drive muscle movement. The ATP is bound in a sort of “pocket” in the protein. The pocket lowers the energy barrier for splitting the ATP – this process of lowering is known as catalysis – and ensures that the desired chemical reaction ensues and ultimately energy is released. The “catalytic pocket” is the biological equivalent of the spark plug in the combustion engine, according to Dr. Fischer.

The existence of this “biological spark plug” has been known for more than 50 years, but researchers have never been able to fully explain how it works, as Stefan Fischer emphasises: “The reaction takes place in about a trillionth of a second, pushing experimental methods to their limits. This event could not be studied exactly until the computer-assisted methods of scientific computing were applied.”

The scientists first had to identify which of the 6,000 atoms of myosin were essential for catalysis. After comprehensive simulations lasting several years, the researchers identified the role of approximately 200 relevant atoms. Because both the myosin atoms and ATP atoms must move during ATP hydrolysis, the possibilities for movement in three-dimensional space are countless – though only one path leads to the lowest energy barrier. “We had to calculate the paths of all approximately 200 atoms in three dimensions; altogether a problem in 600 dimensions,” says Dr. Fischer.

For their complex calculations, the scientists combined the scientific methods from quantum mechanics with high-performance computers. This allowed them to clarify how the interactions between ATP and myosin are organised in order to lower the energy barrier for splitting ATP. Stefan Fischer explains that the electrostatic charges on the protein atoms are positioned around the ATP in such a way that they modify the electron density of this molecule, making it easier for the ATP fuel to split. “This way we could precisely quantify how much every myosin atom relevant in this process contributed to lowering the energy barrier. Based on these findings we succeeded in clearly formulating the protein’s catalytic strategy.”

The biological spark plug mechanism described by the IWR researchers is not only found in cell motors, but is probably also used in all other protein molecules that use ATP as an energy source, says Dr. Fischer. “Because ATP is the fundamental energy currency of cells, almost all biochemical processes in the body are concerned. In terms of a practical application, our findings may be able to help research on new medications for treating cardiac muscle diseases. Our discoveries may also spur new approaches to treating diseases in which ATP splitting is a part of the biochemistry of the pathological system.”

Original publication:
Farooq Ahmad Kiani and Stefan Fischer: Catalytic Strategy Used By The Myosin Motor To Hydrolyze ATP. PNAS (published online 8 July 8 2014), doi:10.1073/pnas.1401862111

Internet information:
http://www.iwr.uni-heidelberg.de/groups/biocomp/fischer

Contact:
Dr. Stefan Fischer
Interdisciplinary Center for Scientific Computing
Phone: +49 6221 54-8858
stefan.fischer@iwr.uni-heidelberg.de

Communications and Marketing
Press Office
Phone: +49 6221 542311
presse@rektorat.uni-heidelberg.de

Marietta Fuhrmann-Koch | idw - Informationsdienst Wissenschaft
Further information:
http://www.uni-heidelberg.de

Further reports about: ATP Biomolecular Computing mechanical methods motors movement petrol processes

More articles from Life Sciences:

nachricht Unexpected flexibility found in odorant molecules
27.06.2016 | Max-Planck-Institut für Struktur und Dynamik der Materie

nachricht Newly-discovered signal in the cell sets protein pathways to mitochondria
27.06.2016 | Eberhard Karls Universität Tübingen

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Unexpected flexibility found in odorant molecules

High resolution rotational spectroscopy reveals an unprecedented number of conformations of an odorant molecule – a new world record!

In a recent publication in the journal Physical Chemistry Chemical Physics, researchers from the Max Planck Institute for the Structure and Dynamics of Matter...

Im Focus: 3-D printing produces cartilage from strands of bioink

Strands of cow cartilage substitute for ink in a 3D bioprinting process that may one day create cartilage patches for worn out joints, according to a team of engineers. "Our goal is to create tissue that can be used to replace large amounts of worn out tissue or design patches," said Ibrahim T. Ozbolat, associate professor of engineering science and mechanics. "Those who have osteoarthritis in their joints suffer a lot. We need a new alternative treatment for this."

Cartilage is a good tissue to target for scale-up bioprinting because it is made up of only one cell type and has no blood vessels within the tissue. It is...

Im Focus: First experimental quantum simulation of particle physics phenomena

Physicists in Innsbruck have realized the first quantum simulation of lattice gauge theories, building a bridge between high-energy theory and atomic physics. In the journal Nature, Rainer Blatt‘s and Peter Zoller’s research teams describe how they simulated the creation of elementary particle pairs out of the vacuum by using a quantum computer.

Elementary particles are the fundamental buildings blocks of matter, and their properties are described by the Standard Model of particle physics. The...

Im Focus: Is There Life On Mars?

Survivalist back from Space - 18 months on the outer skin of the ISS

A year and a half on the outer wall of the International Space Station ISS in altitude of 400 kilometers is a real challenge. Whether a primordial bacterium...

Im Focus: CWRU physicists deploy magnetic vortex to control electron spin

Potential technology for quantum computing, keener sensors

Researchers at Case Western Reserve University have developed a way to swiftly and precisely control electron spins at room temperature.

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ERES 2016: The largest conference in the European real estate industry

09.06.2016 | Event News

Networking 4.0: International Laser Technology Congress AKL’16 Shows New Ways of Cooperations

24.05.2016 | Event News

Challenges of rural labor markets

20.05.2016 | Event News

 
Latest News

Four newly-identified genes could improve rice

27.06.2016 | Agricultural and Forestry Science

Scientists begin modeling universe with Einstein's full theory of general relativity

27.06.2016 | Physics and Astronomy

Newly-discovered signal in the cell sets protein pathways to mitochondria

27.06.2016 | Life Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>