Let's stretch... Scientists study myomesin protein

Feb 14, 2012

The proteins actin, myosin and titin are big players in the business of muscle contraction. Scientists at the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, have now examined another muscle protein – myomesin – which they discovered can stretch up to two-and-a-half times its length, unfolding in a way that was previously unknown. The study is published 14 February in the open-access, online journal PLoS Biology.

Myomesin links muscle filaments, which stretch and contract, so it has to be elastic. Matthias Wilmanns, Head of EMBL Hamburg, and colleagues at the Technical University of Munich in Germany, and The Institute of Cancer Research in the UK, used X-ray crystallography, small-angle X-ray scattering, electron microscopy and atomic force microscopy to reveal the mechanism behind the protein's ability to stretch. The stretchy part of myomesin, analysed by Wilmanns and colleagues, is like a string of pearls, with immunoglobulin (Ig) domains spaced out along an elastic band of structures known as alpha helices.

This video is not supported by your browser at this time.
When myomesin is pulled, as it is when muscles contract and extend, its helices (green) unfold. This strategy, discovered by scientists at EMBL Hamburg, enables the elastic part of the protein to stretch to two and a half times its original length. Published in PLoS Biology on Feb. 14 2012. More information: www.embl.org/press/2012/20120214_Hamburg. Credit: EMBL/Wilmanns

"Looking at these alpha helices was self-suggestive in itself," says Wilmanns. When the is pulled, the helices unfold, whereas the Ig domains do not – a finding that could help to solve an ongoing debate in the field about the potential elasticity of Ig domains.

Next, Wilmanns and his group would like to explore myomesin's role in the body and how it interacts and communicates with other muscle components.

Explore further: Fighting bacteria—with viruses

More information: Pinotsis N, Chatziefthimiou SD, Berkemeier F, Beuron F, Mavridis IM, et al. (2012) Superhelical Architecture of the Myosin Filament-Linking Protein Myomesin with Unusual Elastic Properties. PLoS Biol 10(2): e1001261. doi:10.1371/journal.pbio.1001261

add to favorites email to friend print save as pdf

Related Stories

Muscular protein bond -- strongest yet found in nature

Jul 20, 2009

A research collaboration between Munich-based biophysicists and a structural biologist in Hamburg (Germany) is helping to explain why our muscles, and those of other animals, don't simply fall apart under stress. Their findings ...

How to shoot the messenger

Jan 26, 2010

Cells rely on a range of signaling systems to communicate with each other and to control their own internal workings. Scientists from the European Molecular Biology Laboratory (EMBL) in Hamburg, Germany, have ...

Secrets of water bug wings shed light on heart beats

Dec 07, 2010

A research, led by R.J. Perz-Edwards, Ph.D., of Duke University Medical Center, explains how insect flight muscle works, in particular how insects accomplish something called 'stretch activation,' which has been a scientific ...

Proteins as Parents

Jul 31, 2006

So that we can move, and so that our heart beats, we need proteins with special mechanical properties, "molecular springs", which give our tissues the necessary strength and take care of elasticity and tensibility.

Scientists flex their muscles to solve an old problem

Apr 11, 2011

(PhysOrg.com) -- In a famous experiment first performed more than 220 years ago, Italian physician Luigi Galvani discovered that the muscles of a frog's leg twitch when an electric voltage is applied. An international ...

Recommended for you

Fighting bacteria—with viruses

9 hours ago

Research published today in PLOS Pathogens reveals how viruses called bacteriophages destroy the bacterium Clostridium difficile (C. diff), which is becoming a serious problem in hospitals and healthcare institutes, due to its re ...

Atomic structure of key muscle component revealed

10 hours ago

Actin is the most abundant protein in the body, and when you look more closely at its fundamental role in life, it's easy to see why. It is the basis of most movement in the body, and all cells and components ...

Brand new technology detects probiotic organisms in food

Jul 23, 2014

In the food industr, ity is very important to ensure the quality and safety of products consumed by the population to improve their properties and reduce foodborne illness. Therefore, a team of Mexican researchers ...

Protein evolution follows a modular principle

Jul 23, 2014

Proteins impart shape and stability to cells, drive metabolic processes and transmit signals. To perform these manifold tasks, they fold into complex three-dimensional shapes. Scientists at the Max Planck ...

Report on viruses looks beyond disease

Jul 22, 2014

In contrast to their negative reputation as disease causing agents, some viruses can perform crucial biological and evolutionary functions that help to shape the world we live in today, according to a new report by the American ...

User comments : 0