So says a study published in Nature Communications and conducted by a team of researchers led by Andrea Markelz the University of Buffalo in upstate New York. Using a technique that they themselves have developed, the researchers observed for the first time in detail the vibrations of lysozyme, an antibacterial protein found in many animals. The team found that the vibrations, which previously was thought to deteriorate rapidly, in fact persist in the molecules as the “sound of a bell.”

“These small movements – said Markelz – allow the protein to change shape quickly so that you can easily bind to other proteins, a process that is necessary for our body to perform critical biological functions such as absorbing oxygen, other cells repair and replicate the genetic code. “The research opens the door to a new way of studying the fundamental cellular processes that are the ones that make life possible. The technique could be applied in the future to document how natural or artificial inhibitors block the vital functions that proteins perform. “We can now – he concluded Markelz – try to understand the real structural mechanisms underlying these biological processes and how they are controlled.”

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