Seattle’s Jain Foundation and the University of Washington launch new
Foldit challenge to mark Limb Girdle Muscular Dystrophy Awareness Day,
SEATTLE–(BUSINESS WIRE)–#Foldit–Gamers who have helped scientists understand the structure of hundreds
of complex proteins by playing an online protein folding game Foldit are
being invited to help work out the structure of an abnormal protein that
causes a disabling muscle disorder called limb girdle muscular
dystrophy. The project hopes to enlist thousands of volunteers from
around the world to help determine the shape of the protein that lies at
the root of the disease.
Limb girdle muscular dystrophy, or LGMD, is a rare, inherited disorder
that primarily affects the muscles of the upper arms and legs. As the
disease progresses, it becomes increasingly difficult for people with
LGMD to perform such common activities as lifting objects, standing up
from a chair, or climbing stairs. As the disease progresses, it becomes
increasingly disabling. Currently there is no effective treatment or
“This project is a great opportunity for us to build awareness of this
rare disease and improve our understanding of its causes,” said Dr.
Bradley Williams, director of Research & Diagnostic Innovation at the
foundation and an LGMD patient.
Proteins are made of a string of molecules, called amino acids, which
are linked together like beads on a string. The sequence of the amino
acids determines the folded shape a protein takes, which in turn
determines how the protein works. In order for proteins to function
properly they must fold into the right shape. If they don’t, they won’t
work well, if at all, which can result in disease.
In the new project, which will be launched on Limb Girdle Muscular
Dystrophy Awareness Day, Friday, Sept. 30, the Foldit players will focus
on a protein called dysferlin that is believed to help maintain muscle
cells and allow them to recover from injury.
People who inherit genes responsible for one form of LGMD, called
LGMD-2B, cannot make normal dysferlin. As a result, they become weaker
and weaker as their muscles gradually deteriorate.
The goal of the project is to work out the structure of dysferlin to
better understand how it functions and what other proteins it interacts
with. This information could lead to better treatments and perhaps a
cure. LGMD-2B is a special interest of the Jain Foundation, which was
founded by Ajit Jain, whose son has the disease.
Although it is often possible to predict the shapes proteins will assume
with computer programs that can calculate complex interactions between
amino acids within the protein chain, it turns out that humans, with
their creativity, intuition and their acute spatial awareness, often can
solve protein-folding problems that computers alone cannot.
To harness these abilities, protein researchers at UW Medicine
collaborated with the University of Washington Center for Game Science
to design Foldit, an online computer game. This game allows citizen
scientists working from their home computers to manipulate computer
models of proteins to try to arrive at the shape the proteins most
likely assume in nature.
Since the game was launched in 2009, more than 400,000 Foldit gamers,
most of whom have no scientific background, have had the results of
their team work published in major scientific journals such as Nature,
Science and the Proceedings of the National Academy of Sciences.
“We are optimistic that the creative approaches of our 400,000 Foldit
players will accelerate our ability to understand dysferlin’s function
and lead us to better treatments for muscular dystrophy,” said UW
Medicine researcher Dr. David Baker. A UW professor of biochemistry and
a Howard Hughes Medical Institute investigator, he heads The UW
Institute for Protein Design.
To learn more about LGMD and the efforts by the Jain Foundation to find
a cure visit www.jain-foundation.org
If you are interested in working on this project or are just curious
about Foldit, visit www.fold.it
The puzzle for this project will be posted on Friday, Sept. 30 at http://fold.it/portal/node/2002878
Hillarie Windish, 425-882-1492