Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

New Technology provides a deep view into protein structures

10.07.2012
Proteins usually carry out their biological function when their polypeptide chain is arranged into a stable three-dimensional structure.

The specific structure of a protein is stabilized by numerous hydrogen bonds that connect individual amino acids. Using an innovative method, namely Nuclear Magnetic Resonance (NMR) spectroscopy in combination with high pressure, Dr. Nisius and Prof. Grzesiek from the Biozentrum of the University of Basel have provided important new insights into the hydrogen bond network of Ubiquitin and its importance for the stability of this model protein. Their findings have now been published in the renowned scientific journal Nature Chemistry.


Under pressure: scientists investigate hydrogen bonds under pressures of up to 2500 bar

Proteins consist of a sequence of amino acids and have important physiological functions, such as catalysis or transport of metabolic products. To perform their physiological role, proteins need to fold their linear amino acid chains into a stable three-dimensional structure. In part, the spatial arrangement is determined by a network of hydrogen bonds. However so far it was unclear to what extent individual hydrogen bonds contribute to the stability of a structure. Using a newly developed high pressure cell and NMR method Dr. Nisius and Prof. Grzesiek could, for the first time, completely characterize the stability of individual hydrogen bonds in the protein Ubiquitin.

Particular stability of key, long-range hydrogen bonds
The stability of a thermodynamic system, such as a protein, can be analyzed by subjecting it to variations in pressure and temperature. Using high resolution NMR methods and a newly developed pressure cell Nisius and Grzesiek have precisely analyzed the contributions of 31 backbone hydrogen bonds to the conformational stability of the model protein Ubiquitin. The pressure cell allows the observation of individual protein hydrogen bonds in the NMR instrument under pressures of up to 2500 bar. The latter is equivalent to the hydrostatic pressure of a water column of 25 km height. Hydrogen bonds spanning small sequence separations between the interacting amino acids were found to be particularly stable, whereas hydrogen bonds that span over larger sequence separations showed generally lower stability. Surprisingly, however, there are exceptions to this rule: hydrogen bonds that connect very important parts of Ubiquitin, can span over large sequence separations and be nevertheless extremely stable. In particular, such unusually stable long-range hydrogen bonds were found in the structural part where Ubiquitin attaches to target proteins. By this covalent attachment, ubiquitin labels misfolded target proteins for degradation and fulfills its function in cellular protein quality control. The specific stabilization of hydrogen bonds at this site is therefore very important to preserve the structural integrity of Ubiquitin during function and to achieve stability for the entire protein.
Future oriented technology: High pressure-NMR
By the high pressure NMR characterization, Nisius and Grzesiek could identify the structural parts of Ubiquitin that are responsible for its unusually high thermodynamic stability. Their study is a further example of the multifaceted and growing range of NMR applications. The technology not only provides information on the three-dimensional structure of biomolecules, but also on their thermodynamic and kinetic characteristics, and thus is a crucial tool to understand biomolecular function at atomic resolution.
Original Article:
Lydia Nisius and Stephan Grzesiek (2012). Key stabilizing elements of protein structure identified through pressure and temperature perturbation of its hydrogen bond network. Nature Chemistry, Published online 8. July, 2012.
Further Information:
Prof. Dr. Stephan Grzesiek, Biozentrum of the University of Basel, Structural Biology & Biophysics, Klingelbergstrasse 50/70, 4056 Basel, Tel: +41 61 267 21 00, E-Mail: stephan.grzesiek@unibas.ch

Dr. Thomas Schnyder | Universität Basel
Further information:
http://www.unibas.ch

More articles from Life Sciences:

nachricht 'Y' a protein unicorn might matter in glaucoma
23.10.2017 | Georgia Institute of Technology

nachricht Microfluidics probe 'cholesterol' of the oil industry
23.10.2017 | Rice University

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Salmonella as a tumour medication

HZI researchers developed a bacterial strain that can be used in cancer therapy

Salmonellae are dangerous pathogens that enter the body via contaminated food and can cause severe infections. But these bacteria are also known to target...

Im Focus: Neutron star merger directly observed for the first time

University of Maryland researchers contribute to historic detection of gravitational waves and light created by event

On August 17, 2017, at 12:41:04 UTC, scientists made the first direct observation of a merger between two neutron stars--the dense, collapsed cores that remain...

Im Focus: Breaking: the first light from two neutron stars merging

Seven new papers describe the first-ever detection of light from a gravitational wave source. The event, caused by two neutron stars colliding and merging together, was dubbed GW170817 because it sent ripples through space-time that reached Earth on 2017 August 17. Around the world, hundreds of excited astronomers mobilized quickly and were able to observe the event using numerous telescopes, providing a wealth of new data.

Previous detections of gravitational waves have all involved the merger of two black holes, a feat that won the 2017 Nobel Prize in Physics earlier this month....

Im Focus: Smart sensors for efficient processes

Material defects in end products can quickly result in failures in many areas of industry, and have a massive impact on the safe use of their products. This is why, in the field of quality assurance, intelligent, nondestructive sensor systems play a key role. They allow testing components and parts in a rapid and cost-efficient manner without destroying the actual product or changing its surface. Experts from the Fraunhofer IZFP in Saarbrücken will be presenting two exhibits at the Blechexpo in Stuttgart from 7–10 November 2017 that allow fast, reliable, and automated characterization of materials and detection of defects (Hall 5, Booth 5306).

When quality testing uses time-consuming destructive test methods, it can result in enormous costs due to damaging or destroying the products. And given that...

Im Focus: Cold molecules on collision course

Using a new cooling technique MPQ scientists succeed at observing collisions in a dense beam of cold and slow dipolar molecules.

How do chemical reactions proceed at extremely low temperatures? The answer requires the investigation of molecular samples that are cold, dense, and slow at...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

3rd Symposium on Driving Simulation

23.10.2017 | Event News

ASEAN Member States discuss the future role of renewable energy

17.10.2017 | Event News

World Health Summit 2017: International experts set the course for the future of Global Health

10.10.2017 | Event News

 
Latest News

Microfluidics probe 'cholesterol' of the oil industry

23.10.2017 | Life Sciences

Gamma rays will reach beyond the limits of light

23.10.2017 | Physics and Astronomy

The end of pneumonia? New vaccine offers hope

23.10.2017 | Health and Medicine

VideoLinks
B2B-VideoLinks
More VideoLinks >>>