Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:


Conserved amino acids play both structural and mechanistic roles in sandwich-like protein


Scientists at Rice University report their findings in PNAS

The question of whether amino acids in sandwich-like proteins are there to stabilize the structure or to speed up the protein-folding process is best answered by "all of the above," according to researchers at Rice University in Houston. This discovery, reported in today’s issue of the Proceedings of the National Academy of Sciences, could benefit future research on treatments for diseases related to misfolded proteins, such as Alzheimer’s and Huntington’s.

The Rice scientists studied azurin – a copper-containing protein essential to electron transfer. Azurin is part of a group of proteins that fold into a sandwich-like structure consisting of two sheets of amino acids meshed together. Nearly 70 superfamilies of proteins of varying makeup have this sandwich-like structure, but they all have eight particular amino acids in common. Previous studies had shown that these eight amino acids were important to define the sandwich-like structure, but the exact role was unknown.

"Why are these eight amino acids invariant across all sandwich-like proteins?" asked principal investigator Pernilla Wittung-Stafshede, associate professor of biochemistry and cell biology. "Are they conserved to direct the protein-folding reaction, or are they selected to stabilize the final protein structure? In our paper, we unravel an unprecedented answer to this question."

Wittung-Stafshede and graduate student Corey Wilson analyzed the purpose of six of the eight amino acids by exchanging a nonessential amino acid for each of them and monitoring the effect on the protein structure. (For technical reasons, the other two amino acids could not be studied.) The researchers found that three of the amino acids are important for stabilizing the final structure of the protein, and three serve to direct the process of protein folding.

"We directly demonstrated that in one protein within the large sandwich-like protein family, evolution has indeed preserved amino acids for mechanical reasons," Wittung-Stafshede said. "We believe that our discovery is novel and that it gives important new insight into the interplay between protein evolution, structure and folding."

The researchers speculate that their conclusions about the azurin protein apply to most members of the sandwich-like protein family, but testing on other specific proteins must confirm that.

"Better understanding of protein folding is crucial for curing human diseases directly related to misfolding of proteins, and it is also important for the design and improvement of therapeutic enzymes," Wittung-Stafshede said.

B.J. Almond | EurekAlert!
Further information:

More articles from Life Sciences:

nachricht Biologists unravel another mystery of what makes DNA go 'loopy'
16.03.2018 | Emory Health Sciences

nachricht Scientists map the portal to the cell's nucleus
16.03.2018 | Rockefeller 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: Locomotion control with photopigments

Researchers from Göttingen University discover additional function of opsins

Animal photoreceptors capture light with photopigments. Researchers from the University of Göttingen have now discovered that these photopigments fulfill an...

Im Focus: Surveying the Arctic: Tracking down carbon particles

Researchers embark on aerial campaign over Northeast Greenland

On 15 March, the AWI research aeroplane Polar 5 will depart for Greenland. Concentrating on the furthest northeast region of the island, an international team...

Im Focus: Unique Insights into the Antarctic Ice Shelf System

Data collected on ocean-ice interactions in the little-researched regions of the far south

The world’s second-largest ice shelf was the destination for a Polarstern expedition that ended in Punta Arenas, Chile on 14th March 2018. Oceanographers from...

Im Focus: ILA 2018: Laser alternative to hexavalent chromium coating

At the 2018 ILA Berlin Air Show from April 25–29, the Fraunhofer Institute for Laser Technology ILT is showcasing extreme high-speed Laser Material Deposition (EHLA): A video documents how for metal components that are highly loaded, EHLA has already proved itself as an alternative to hard chrome plating, which is now allowed only under special conditions.

When the EU restricted the use of hexavalent chromium compounds to special applications requiring authorization, the move prompted a rethink in the surface...

Im Focus: Radar for navigation support from autonomous flying drones

At the ILA Berlin, hall 4, booth 202, Fraunhofer FHR will present two radar sensors for navigation support of drones. The sensors are valuable components in the implementation of autonomous flying drones: they function as obstacle detectors to prevent collisions. Radar sensors also operate reliably in restricted visibility, e.g. in foggy or dusty conditions. Due to their ability to measure distances with high precision, the radar sensors can also be used as altimeters when other sources of information such as barometers or GPS are not available or cannot operate optimally.

Drones play an increasingly important role in the area of logistics and services. Well-known logistic companies place great hope in these compact, aerial...

All Focus news of the innovation-report >>>



Industry & Economy
Event News

Ultrafast Wireless and Chip Design at the DATE Conference in Dresden

16.03.2018 | Event News

International Tinnitus Conference of the Tinnitus Research Initiative in Regensburg

13.03.2018 | Event News

International Virtual Reality Conference “IEEE VR 2018” comes to Reutlingen, Germany

08.03.2018 | Event News

Latest News

Wandering greenhouse gas

16.03.2018 | Earth Sciences

'Frequency combs' ID chemicals within the mid-infrared spectral region

16.03.2018 | Physics and Astronomy

Biologists unravel another mystery of what makes DNA go 'loopy'

16.03.2018 | Life Sciences

Science & Research
Overview of more VideoLinks >>>