Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:


Researchers Solve Complex Problem in Membrane Biochemistry Through Study of Amino Acids

After years of experimentation, researchers at the University of Arkansas have solved a complex, decades-old problem in membrane biochemistry. The consequence of their work will give scientists more information about the function and structure of proteins, the workhorses within the cells of the human body.

“Historically, lysine and arginine, both basic amino acids, were considered to have very similar properties and therefore to be essentially interchangeable,” said Denise Greathouse, a research associate professor in the department of chemistry and biochemistry. “Our results demonstrate that despite their similarities, the differences in their behavior in membrane environments provide important clues for understanding membrane protein function.”

The findings, which appear in the January issue of the journal Proceedings of the National Academy of Sciences, address long-standing questions in the study of protein structure and function and help explain how charged amino acids are able to modulate the behavior of proteins in cellular membranes.

Greathouse, former doctoral students Nicholas Gleason and Vitaly Vostrikov, and Roger Koeppe II, Distinguished Professor of chemistry and biochemistry, wrote the article, “Buried lysine, but not arginine, titrates and alters transmembrane helix tilt.”

Proteins do nearly all the work in the cells of our bodies, ranging from brain function and nerve transmission to metabolic energy production and muscular contraction. Moreover, many diseases are associated with defects in protein function. Future advances in the diagnosis and treatment of human disease will depend upon better understanding of the thousands of proteins that are encoded within the genomes of humans and human pathogens.

The structure and function of membrane proteins both play a crucial role in cell signaling and the regulation of biological function. The authors developed experimental methods that determine how lysine and arginine interact in the lipid bilayer membrane environment. In the last 10 years there have been computational predictions of the behavior of lysine and arginine in the membrane but not methods to test those predictions.

“It is the first measurement of its type, its complexity makes it an elegant method, and it opens the door for other people to apply these methods on biologically important problems,” Koeppe said. “There is a lot of interest in trying to understand what’s going on in these membranes, especially with protein molecules that carry particular electric charges. Unless we can understand it at the fundamental level, then we can’t extrapolate it to the nervous system. We’re trying to develop foundational knowledge that is needed to understand the nervous system.

“We’re excited about this study because it makes available knowledge that other researchers can use,” he said. “Those making the computer predictions can refine their methods and make better predictions because they know that they were able to reproduce some of our results.”

Lysine and arginine are ionizable, which means they can have a positive electric charge. The research team created a framework for experimentation that uses magnetic resonance imaging to measure whether the groups remain charged or become uncharged as the acidity or the pH of the environment is changed. To make their procedure work, the scientists synthesized peptides, which are chemical compounds consisting of several or more linked amino acids. To enable the magnetic resonance experiments, some of the hydrogen atoms in the peptides were replaced with deuterium, a heavy isotope of hydrogen.

“We’ve spent about 15 years doing this,” Koeppe said. “We developed first- and second-generation families of model peptides, and we examine them in model lipid membranes in order to understand the properties of real cell membranes and real cell proteins. This is at a molecular level. We are not even up to the cell yet.”

Vostrikov and Gleason earned their doctorates in 2011 and 2012, respectively. Vostrikov is a postdoctoral fellow at the University of Minnesota and Gleason teaches chemistry at Shiloh Christian School in Springdale.

The National Science Foundation provided the grant for the experiments described in the Proceedings of the National Academy of Sciences. The National Institutes of Health provided the financial support for the early stages of development of the peptide framework and for the facilities.

The research was performed in the U of A’s Center for Protein Structure and Function, which was established in 2000 in the J. William Fulbright College of Arts and Sciences to develop a detailed understanding of the structure and function of proteins that could lead to improved treatments of human disease. Center scientists study proteins involved in cancer, heart disease, osteoporosis, the flu and other diseases and conditions.


Roger Koeppe II, Distinguished Professor, chemistry and biochemistr
J. William Fulbright College of Arts and Sciences

Roger Koeppe | Newswise
Further information:

More articles from Life Sciences:

nachricht Novel mechanisms of action discovered for the skin cancer medication Imiquimod
21.10.2016 | Technische Universität München

nachricht Second research flight into zero gravity
21.10.2016 | Universität Zürich

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: New 3-D wiring technique brings scalable quantum computers closer to reality

Researchers from the Institute for Quantum Computing (IQC) at the University of Waterloo led the development of a new extensible wiring technique capable of controlling superconducting quantum bits, representing a significant step towards to the realization of a scalable quantum computer.

"The quantum socket is a wiring method that uses three-dimensional wires based on spring-loaded pins to address individual qubits," said Jeremy Béjanin, a PhD...

Im Focus: Scientists develop a semiconductor nanocomposite material that moves in response to light

In a paper in Scientific Reports, a research team at Worcester Polytechnic Institute describes a novel light-activated phenomenon that could become the basis for applications as diverse as microscopic robotic grippers and more efficient solar cells.

A research team at Worcester Polytechnic Institute (WPI) has developed a revolutionary, light-activated semiconductor nanocomposite material that can be used...

Im Focus: Diamonds aren't forever: Sandia, Harvard team create first quantum computer bridge

By forcefully embedding two silicon atoms in a diamond matrix, Sandia researchers have demonstrated for the first time on a single chip all the components needed to create a quantum bridge to link quantum computers together.

"People have already built small quantum computers," says Sandia researcher Ryan Camacho. "Maybe the first useful one won't be a single giant quantum computer...

Im Focus: New Products - Highlights of COMPAMED 2016

COMPAMED has become the leading international marketplace for suppliers of medical manufacturing. The trade fair, which takes place every November and is co-located to MEDICA in Dusseldorf, has been steadily growing over the past years and shows that medical technology remains a rapidly growing market.

In 2016, the joint pavilion by the IVAM Microtechnology Network, the Product Market “High-tech for Medical Devices”, will be located in Hall 8a again and will...

Im Focus: Ultra-thin ferroelectric material for next-generation electronics

'Ferroelectric' materials can switch between different states of electrical polarization in response to an external electric field. This flexibility means they show promise for many applications, for example in electronic devices and computer memory. Current ferroelectric materials are highly valued for their thermal and chemical stability and rapid electro-mechanical responses, but creating a material that is scalable down to the tiny sizes needed for technologies like silicon-based semiconductors (Si-based CMOS) has proven challenging.

Now, Hiroshi Funakubo and co-workers at the Tokyo Institute of Technology, in collaboration with researchers across Japan, have conducted experiments to...

All Focus news of the innovation-report >>>



Event News

#IC2S2: When Social Science meets Computer Science - GESIS will host the IC2S2 conference 2017

14.10.2016 | Event News

Agricultural Trade Developments and Potentials in Central Asia and the South Caucasus

14.10.2016 | Event News

World Health Summit – Day Three: A Call to Action

12.10.2016 | Event News

Latest News

Resolving the mystery of preeclampsia

21.10.2016 | Health and Medicine

Stanford researchers create new special-purpose computer that may someday save us billions

21.10.2016 | Information Technology

From ancient fossils to future cars

21.10.2016 | Materials Sciences

More VideoLinks >>>