University of Wisconsin-Madison biochemists have developed an approach that allows them to measure with unprecedented accuracy the strengths of hydrogen bonds in a protein. The scientists were then able to predict the function of different versions of the protein based on structural information, a novel outcome that was published recently in the Proceedings of the National Academy of Sciences.
Professor of biochemistry John Markley, along with a team that included graduate student I-Jin Lin, studied iron-sulfur proteins called rubredoxins that transfer energy in the form of electrons throughout living systems.
Rubredoxin is a key part of processes like photosynthesis and respiration, where energy is converted from one form to another.
"Variants of rubredoxin have evolved different sequences to transport electrons in the most efficient manner possible," Markley explains. "Different mechanisms have been put forward to explain this, and we wanted to understand how the proteins evolved to have different electron affinities."
John Markley | EurekAlert!
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Spectrally narrow x-ray pulses may be “sharpened” by purely mechanical means. This sounds surprisingly, but a team of theoretical and experimental physicists developed and realized such a method. It is based on fast motions, precisely synchronized with the pulses, of a target interacting with the x-ray light. Thereby, photons are redistributed within the x-ray pulse to the desired spectral region.
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