Featured Research

from universities, journals, and other organizations

Force Governs Function Of Proteins

Date:
March 12, 2008
Source:
ETH Zurich
Summary:
Today nanotechnology enables us to attract individual molecules mechanically, allowing their behavior when exposed to a mechanical force to be observed. With the aid of computer simulations, researchers can now illustrate how a particular scaffolding protein in the bonding between the extra-cellular matrix and the internal cytoskeleton can be activated by exerting force upon it.

Talin (blue) is an important scaffolding protein that binds the contractile cytoskeleton to the extra-cellular matrix via integrins. Its structure consists of a bundle of many tightly packed alpha helixes. If a cell sticks to a surface, thus exerting forces upon the scaffolding protein, the helix bundle breaks, exposing the helixes that can only bind vinculin after this "activation".
Credit: Image courtesy of ETH Zurich

Today nanotechnology enables us to attract individual molecules mechanically, allowing their behaviour when exposed to a mechanical force to be observed. With the aid of computer simulations, ETH Zurich researchers can now illustrate how a particular scaffolding protein in the bonding between the extra-cellular matrix and the internal cytoskeleton can be activated by exerting force upon it.

For a cell to survive, most eukaryotes have to be anchored to their surroundings mechanically. This is achieved by special proteins, the integrins, which cross the cell membrane. They are connected to the external periphery of the cell, the so-called extra-cellular matrix, and the cell interior, the cytoskeleton, by scaffolding proteins such as talin. Vesa Hytönen, a post-doc at the Laboratory for Biologically Oriented Materials at ETH Zurich, and Viola Vogel, Professor of Biologically Oriented Materials, also at ETH Zurich, have succeeded in revealing a mechanism as to how the scaffolding protein can recruit the protein vinculin when exposed to a force and bind with it. In a state of equilibrium, talin would not do this without force.

Water activates restructuring

The researchers can now demonstrate on an atomic scale how the structure of the scaffolding protein talin changes if force is exerted upon it using high-resolution computer simulations. Talin consists of several tightly packed helix bundles. If it is stretched mechanically, the bundles break into several smaller bundles that remain interconnected. Consequently, in the case of talin, vinculin binding sites located on hidden helixes are laid open. This happens when water molecules infiltrate the talin and moisten the hydrophobic sections of individual talin helixes.

As these helixes have an aversion to water, they try to hide their hydrophobic sections by forming complexes with other proteins – in this case, vinculin. Water thus activates the structural exchange of an entire talin helix, which is still bound like a washing line at the ends with talin but which structurally forms a complex with vinculin. According to Viola Vogel, vinculin’s complementary helix bundle structure makes this possible. Like talin, vinculin can then also connect to the cytoskeleton and thus mechanically reinforce the scaffolding between the interior and exterior.

“Previously, research primarily concentrated on the relationship between the structure and function of proteins that are in equilibrium with their surroundings”, explains Viola Vogel. For the last few decades, as nanotechnology established itself and began to be researched in billionths of a meter, it has been possible to investigate the mechanical properties of proteins and pursue the question as to how mechanical forces govern the way the proteins work.

New field of research

Vogel states that the new computerized results explain all previous laboratory experiments. Today, we only know how very few proteins are altered biochemically or even activated and deactivated by mechanical forces. The fact that proteins can be activated by mechanical forces by exchanging a helix, however, is still something special. According to Vogel, there is still a lot of work to be done in this new field of research. In future, these results might be used in biotechnology or medicine.

Journal eference: Hytönen, V. & Vogel, V.: How Force Might Activate Talin’s Vinculin Binding Sites: SMD Reveals a Structural Mechanism, PLoS Computational Biology 4 (2008), doi:10.1371/journal.pcbi.0040024

 


Story Source:

The above story is based on materials provided by ETH Zurich. Note: Materials may be edited for content and length.


Cite This Page:

ETH Zurich. "Force Governs Function Of Proteins." ScienceDaily. ScienceDaily, 12 March 2008. <www.sciencedaily.com/releases/2008/03/080307102046.htm>.
ETH Zurich. (2008, March 12). Force Governs Function Of Proteins. ScienceDaily. Retrieved April 20, 2014 from www.sciencedaily.com/releases/2008/03/080307102046.htm
ETH Zurich. "Force Governs Function Of Proteins." ScienceDaily. www.sciencedaily.com/releases/2008/03/080307102046.htm (accessed April 20, 2014).

Share This



More Matter & Energy News

Sunday, April 20, 2014

Featured Research

from universities, journals, and other organizations


Featured Videos

from AP, Reuters, AFP, and other news services

Why Did Nike Fire Most Of Its Nike FuelBand Team?

Why Did Nike Fire Most Of Its Nike FuelBand Team?

Newsy (Apr. 19, 2014) — Nike fired most of its Digital Sport hardware team, the group behind Nike's FuelBand device. Could Apple or an overcrowded market be behind layoffs? Video provided by Newsy
Powered by NewsLook.com
Small Reactors Could Be Future of Nuclear Energy

Small Reactors Could Be Future of Nuclear Energy

AP (Apr. 17, 2014) — After the Fukushima nuclear disaster, the industry fell under intense scrutiny. Now, small underground nuclear power plants are being considered as the possible future of the nuclear energy. (April 17) Video provided by AP
Powered by NewsLook.com
Horseless Carriage Introduced at NY Auto Show

Horseless Carriage Introduced at NY Auto Show

AP (Apr. 17, 2014) — An electric car that proponents hope will replace horse-drawn carriages in New York City has also been revealed at the auto show. (Apr. 17) Video provided by AP
Powered by NewsLook.com
Honda's New ASIMO Robot, More Human-Like Than Ever

Honda's New ASIMO Robot, More Human-Like Than Ever

AFP (Apr. 17, 2014) — It walks and runs, even up and down stairs. It can open a bottle and serve a drink, and politely tries to shake hands with a stranger. Meet the latest ASIMO, Honda's humanoid robot. Duration: 00:54 Video provided by AFP
Powered by NewsLook.com

Search ScienceDaily

Number of stories in archives: 140,361

Find with keyword(s):
 
Enter a keyword or phrase to search ScienceDaily for related topics and research stories.

Save/Print:
Share:  

Breaking News:
from the past week

In Other News

... from NewsDaily.com

Science News

Health News

Environment News

Technology News



Save/Print:
Share:  

Free Subscriptions


Get the latest science news with ScienceDaily's free email newsletters, updated daily and weekly. Or view hourly updated newsfeeds in your RSS reader:

Get Social & Mobile


Keep up to date with the latest news from ScienceDaily via social networks and mobile apps:

Have Feedback?


Tell us what you think of ScienceDaily -- we welcome both positive and negative comments. Have any problems using the site? Questions?
Mobile iPhone Android Web
Follow Facebook Twitter Google+
Subscribe RSS Feeds Email Newsletters
Latest Headlines Health & Medicine Mind & Brain Space & Time Matter & Energy Computers & Math Plants & Animals Earth & Climate Fossils & Ruins