Corporate Banner
Satellite Banner
Proteomics
Scientific Community
 
Become a Member | Sign in
Home>News>This Article
  News
Return

Proteins in their Natural Habitat

Published: Wednesday, October 30, 2013
Last Updated: Wednesday, October 30, 2013
Bookmark and Share
Proteins which reside in the membrane of cells play a key role in many biological processes and provide targets for more than half of current drug treatments.

These membrane proteins are notoriously difficult to study in their natural environment, but scientists at the University of Oxford have now developed a technique to do just that, combining the use of sophisticated nanodiscs and mass spectrometers.

Mass spectrometry is a technique which allows scientists to probe molecular interactions. Using a high-tech 'nanoflow' system, molecules are transmitted into the instrument in charged water droplets, which then undergo evaporation releasing molecules into the gas phase of the mass spectrometer.

But membrane proteins are difficult to measure in this way, as they are hydrophobic: they don't dissolve in water. One way to overcome this problem is to mix them with detergents. Detergents work by surrounding insoluble substances with a water-friendly shell. Each detergent particle has two ends – the heads are attracted to water and the tails are attracted to insoluble regions of the membrane protein. The tails stick to the hydrophobic parts, leaving a shell of water-loving heads around the outside. The molecules can then easily dissolve in water.

Although detergents can be used to get membrane proteins to dissolve in water, these artificial chemicals can damage protein structures and do not faithfully mimic the natural environments in which they are normally found. The Oxford group, led by Professor Carol Robinson, has utilised a technique which allows them to study membrane protein structures by mass spectrometry from their natural environment. Their new method, published in Nature Methods, uses tiny disc-like structures made from molecules called lipids, as first author Dr Jonathan Hopper explains:

'Membrane proteins are naturally found in flat structures called lipid bilayers. Lipids are a bit like nature's detergents, in that they have water-loving heads and fat-loving tails. Lipid bilayers are made up of two sheets of lipids with their tails pointing inwards.

'The nanodiscs we use are made from lipids, the same material that membrane proteins occupy in the body. It's essentially as if you took a round cookie cutter to remove a section of the natural bilayer, so the conditions are just like they would be in the body. The discs are stabilised by wrapping a belt of proteins around them to keep the exposed lipid tails from the water.

'Aside from the nanodiscs, we actually got great results from 'bicelles', which are made in a similar way.  The main difference is that instead of putting a belt of proteins around the edge, we plug the gap with short-chain lipids instead. This actually gives us much more control over the size and structure of the disc.'

These innovations enable researchers to study membrane protein structures using sophisticated mass spectrometry, in environments as close to the human body as possible.

'I am delighted that this has worked, it is completely unexpected given the difficulties we have had in the past in studying these complexes in lipidic environments,' says study leader Professor Carol Robinson. 'The breakthrough enables us to study membrane proteins in a natural environment for the first time. We believe this will have a great impact on structural biology approaches, and could in turn lead to better-designed drug treatments.'


Further Information

Join For Free

Access to this exclusive content is for Technology Networks Premium members only.

Join Technology Networks Premium for free access to:

  • Exclusive articles
  • Presentations from international conferences
  • Over 3,200+ scientific posters on ePosters
  • More than 4,800+ scientific videos on LabTube
  • 35 community eNewsletters


Sign In



Forgotten your details? Click Here
If you are not a member you can join here

*Please note: By logging into TechnologyNetworks.com you agree to accept the use of cookies. To find out more about the cookies we use and how to delete them, see our privacy policy.


Scientific News
Liquid Biopsies: Miracle Diagnostic or Next New Fad?
Thanks to the development of highly specific gene-amplification and sequencing technologies liquid biopsies access more biomarkers relevant to more cancers than ever before.
Cell Cargo Ships in Near Future?
Virus-inspired container design may lead to cell cargo ships following construction of ten large, two-component, icosahedral protein complexes.
Protein Reinforces Growth of Damaged Muscles
Biologists have found a protein involved in stem cells that bolsters damaged muscle tissue growth - potential for muscle degeneration treatments.
Structure of Cold Virus Solved
Researchers have identified the structure of an elusive cold virus linked to child asthma and respiratory infections, providing the foundation for treating the virus.
New Protein Model Could Accelerate Drug Development
Stony Brook-led international research team creates ultra-fast approach to model protein interactions.
Researchers Can Control Genes Involved in Cancer
A new way to control the activity of a protein, that is often upregulated in cancer, has been discovered by Moffitt researchers through monoubiquitination mechanism.
Mitochondrial Role in Metastatic Cancer
Researchers have manipulated proteins, sourced from tumour cells, that are essential for maintaining tumour cells and in doing so, have significantly reduced the ability of cancer cells.
Liquid Biopsy Predicts Colon Cancer Recurrence
Scientists have used a genetic test that spots bits of cancer-related DNA circulating in the blood to accurately predict the likelihood of the disease’s return in some — but not all — of a small group of patients with early-stage colon cancer.
Scientists Culture Elusive Yellowstone Microbe
ORNL scientists have successfully isolated and cultured a Yellowstone sourced acidic hot-spring based microbe.
Seeing RNA at the Nanoscale
MIT researchers have developed a new way to image proteins and RNA inside neurons of brain tissue.
Scroll Up
Scroll Down
SELECTBIO

SELECTBIO Market Reports
Go to LabTube
Go to eposters
 
Access to the latest scientific news
Exclusive articles
Upload and share your posters on ePosters
Latest presentations and webinars
View a library of 1,800+ scientific and medical posters
3,200+ scientific and medical posters
A library of 2,500+ scientific videos on LabTube
4,800+ scientific videos
Close
Premium CrownJOIN TECHNOLOGY NETWORKS PREMIUM FOR FREE!