Institut Laue-Langevin

Neutrons explain haemoglobin evolution in red blood cells

Scientists have explained the evolutionary history of haemoglobin using what might seem an unlikely array of samples. Researchers focused the world’s most intense neutrons beams on the oxygen-carrying protein from a human, a duck-billed platypus, a chicken and a salt-water crocodile to explain how it has adapted to different body temperatures within different species. The results of research at the Institut Laue-Langevin (ILL), Aachen University of Applied Sciences (FH Aachen), the Australian Nuclear Science and Technology Organisation, the Centre National de la Recherche Scientifique (CNRS) in Paris and the FRMII facility in Germany could lead to interesting developments in bio-engineering and biomedical research.

Haemoglobin is an iron-rich protein found in all vertebrates that carries oxygen from the lungs to the rest of the body. The stiffness of human haemoglobin is ideally suited to our own body temperature– 37 degrees Celsius. Research by Gerhard Artmann at FH Aachen showed that at this temperature it partially unfolds, softening sufficiently for oxygen molecules to penetrate its four iron atoms without completely compromising its structural integrity and collapsing. [more]