A Lawrence Livermore National Laboratory physicist, in collaboration with an international team of researchers, has developed an experimental method that allows scientists to investigate the behavior of proteins under non-equilibrium conditions one molecule at a time, to better understand a fundamental biological process of protein folding that is important for many diseases.
The work, presented in the Aug. 29 edition of Science, marks the first time protein-folding kinetics has been monitored on the single-molecule level. Proteins are long chains of amino acids. Like shoelaces, they loop about each other or fold in a variety of ways, and only one way allows the protein to function properly. Just as a knotted shoelace can be a problem, a misfolded protein can do serious damage. Many diseases, such as Alzheimers, cystic fibrosis, mad cow disease and many cancers result from misfolded protein.
Livermores Lawrence postdoctoral fellow Olgica Bakajin worked with scientists from the NIDDK Laboratory of Chemical Physics at the National Institute of Health and the Physikalische Biochemie Universität Postadam in Germany to develop a microfluidic mixer for studies of protein folding. With this mixer, researchers were able to access information about the protein folding reaction that was never available from ensemble measurements or even from the newer single molecule equilibrium measurements.
Anne Stark | EurekAlert!
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