Navigation Links
The lock shapes the key
Date:2/15/2011

This release is available in German.

Interactions between proteins are of fundamental importance for a number of processes in virtually every living cell. However, in order for the proteins to carry out any biological function, they must first assume their specific three-dimensional shape. A number of reactions have been described in recent years, where one of the interaction partners does not assume its active structure until the actual binding process commences. It was still a great mystery, though, how the binding partners could actually recognize such unstructured proteins.

Scientists led by Professor Thomas Kiefhaber (TUM) posed the question of whether local properties are sufficient for the recognition to take place or whether the unstructured binding partner first had to assume a specific spatial structure. Possible candidates were regularly structural elements such as coiled α-helices or β-pleated sheets, in which internal hydrogen bonds are formed.

In collaboration with Professor Gunter Fischer's research group at the Max Planck Research Unit for Enzymology of Protein Folding Halle/Saale, the scientists developed a novel method for observing the formation of individual hydrogen bonds in the course of a binding process.

The model system was the enzyme ribonuclease S, which in its active form comprises the S-protein and an α-helical S-peptide. While the S-protein has a defined three-dimensional shape, the S-peptide on its own is initially unfolded. The scientists attempted to determine whether the S-protein recognizes the unstructured S-peptide or a small fraction of peptide molecules in their helical conformation. To this end, the oxygen atoms in the peptide bonds were replaced by sulfur atoms via chemical protein synthesis, causing individual hydrogen bonds to become destabilized.

Time-based measurements of the binding process of the altered peptide have now shown that the hydrogen bonds in the S-peptide, and as such in the α-helical structure, do not form until after the bonding to the S-protein. Thus, they cannot play a role in the recognition process. Protein-protein recognition in this case takes place via hydrophobic interaction of the S-protein with two spatially clearly defined areas of the unstructured S-peptide.

These results are of fundamental importance for understanding the mechanism of protein-protein interactions. In the future, this method can be used to examine in detail the structure formation in proteins in other systems, as well.


'/>"/>

Contact: Dr. Andreas Battenberg
battenberg@zv.tum.de
49-892-891-0510
Technische Universitaet Muenchen
Source:Eurekalert

Related biology news :

1. Scientists clock on to how sunlight shapes daily rhythms
2. Oil spill reshapes sweeping new study of oyster reefs -- Virginia to Florida
3. Study finds that long-distance migration shapes butterfly wings
4. Yes, ecology shapes evolution, but guppies show reverse also true
5. Caltech and UCSD researchers shed light on how proteins find their shapes
6. Grape shapes
Post Your Comments:
*Name:
*Comment:
*Email:
(Date:11/30/2016)... 30, 2016 Not many of us realize that we spend ? of ... we need to do it well. Inadequate sleep levels have been found to lead ... diabetes, and even cancer. Maybe now is the best time to rethink ... them to manage their sleep quality? Continue Reading ... ...
(Date:11/28/2016)... Nov. 28, 2016 "The ... of 16.79%" The biometric system market is in ... in the near future. The biometric system market is ... 2022, at a CAGR of 16.79% between 2016 and ... of biometric technology in smartphones, rising use of biometric ...
(Date:11/19/2016)... 2016 Securus Technologies, a leading provider of ... investigation, corrections and monitoring, announced today that it has ... have an independent technology judge determine who has the ... tech/sophisticated telephone calling platform, and the best customer service. ... most of what we do – which clearly is ...
Breaking Biology News(10 mins):
(Date:12/8/2016)... SAN DIEGO, Dec. 8, 2016  OncoSec Medical ... company developing DNA-based intratumoral cancer immunotherapies, today announced ... "We are delivering on our ... melanoma with ImmunoPulse® IL-12. We are pleased with ... melanoma combination trial, and we are focused on ...
(Date:12/8/2016)... , December 8, 2016 AskLinkerReports.com ... comprehensive analysis, titled Global Amyloglucosidase Industry 2016 Market Research Report. ... application, and industry chain overview are all covered in the ... analysis, and investment return analysis of the Amyloglucosidase industry. ... , , ...
(Date:12/8/2016)...  Renova™ Therapeutics, a biotechnology company developing gene ... 2 diabetes, announced that it has obtained a ... vector developed in the laboratory of Professor ... The company plans to use this vector in ... "Early research has shown promise ...
(Date:12/8/2016)... (PRWEB) , ... December 08, 2016 , ... ... light to control cells — optogenetics — is key to exciting advances in ... the art, spatially patterned light projected via free-space optics stimulates small, transparent organisms ...
Breaking Biology Technology: