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 A Map of the Cell’s Power Station
18.08.2017 | Albert-Ludwigs-Universität Freiburg im Breisgau

nachricht On the way to developing a new active ingredient against chronic infections
21.08.2017 | Deutsches Zentrum für Infektionsforschung

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Fizzy soda water could be key to clean manufacture of flat wonder material: Graphene

Whether you call it effervescent, fizzy, or sparkling, carbonated water is making a comeback as a beverage. Aside from quenching thirst, researchers at the University of Illinois at Urbana-Champaign have discovered a new use for these "bubbly" concoctions that will have major impact on the manufacturer of the world's thinnest, flattest, and one most useful materials -- graphene.

As graphene's popularity grows as an advanced "wonder" material, the speed and quality at which it can be manufactured will be paramount. With that in mind,...

Im Focus: Exotic quantum states made from light: Physicists create optical “wells” for a super-photon

Physicists at the University of Bonn have managed to create optical hollows and more complex patterns into which the light of a Bose-Einstein condensate flows. The creation of such highly low-loss structures for light is a prerequisite for complex light circuits, such as for quantum information processing for a new generation of computers. The researchers are now presenting their results in the journal Nature Photonics.

Light particles (photons) occur as tiny, indivisible portions. Many thousands of these light portions can be merged to form a single super-photon if they are...

Im Focus: Circular RNA linked to brain function

For the first time, scientists have shown that circular RNA is linked to brain function. When a RNA molecule called Cdr1as was deleted from the genome of mice, the animals had problems filtering out unnecessary information – like patients suffering from neuropsychiatric disorders.

While hundreds of circular RNAs (circRNAs) are abundant in mammalian brains, one big question has remained unanswered: What are they actually good for? In the...

Im Focus: RAVAN CubeSat measures Earth's outgoing energy

An experimental small satellite has successfully collected and delivered data on a key measurement for predicting changes in Earth's climate.

The Radiometer Assessment using Vertically Aligned Nanotubes (RAVAN) CubeSat was launched into low-Earth orbit on Nov. 11, 2016, in order to test new...

Im Focus: Scientists shine new light on the “other high temperature superconductor”

A study led by scientists of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg presents evidence of the coexistence of superconductivity and “charge-density-waves” in compounds of the poorly-studied family of bismuthates. This observation opens up new perspectives for a deeper understanding of the phenomenon of high-temperature superconductivity, a topic which is at the core of condensed matter research since more than 30 years. The paper by Nicoletti et al has been published in the PNAS.

Since the beginning of the 20th century, superconductivity had been observed in some metals at temperatures only a few degrees above the absolute zero (minus...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Call for Papers – ICNFT 2018, 5th International Conference on New Forming Technology

16.08.2017 | Event News

Sustainability is the business model of tomorrow

04.08.2017 | Event News

Clash of Realities 2017: Registration now open. International Conference at TH Köln

26.07.2017 | Event News

 
Latest News

Nagoya physicists resolve long-standing mystery of structure-less transition

21.08.2017 | Materials Sciences

Chronic stress induces fatal organ dysfunctions via a new neural circuit

21.08.2017 | Health and Medicine

Scientists from the MSU studied new liquid-crystalline photochrom

21.08.2017 | Materials Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>