For decades we’ve heard of the horrific difficulty of the protein folding problem: how to go from knowledge of a linear sequence of amino acids to the three-dimensional structure of a folded, useful protein? This is needed if we are to use proteins to build 3D structures that we want for nanotechnology. From Physorg.com we learn of exciting nanotech progress at Harvard by Eugene Shakhnovich and team:
Comprehensive model is first to map protein folding at atomic level
Scientists at Harvard University have developed a computer model that, for the first time, can fully map and predict how small proteins fold into three-dimensional, biologically active shapes. The work could help researchers better understand the abnormal protein aggregation underlying some devastating diseases, as well as how natural proteins evolved and how proteins recognize correct biochemical partners within living cells…
In more than 4,000 simulations conducted by the researchers, the computer model consistently predicted folded structures nearly identical to those that have been observed experimentally.
“This work should open new vistas in protein engineering, allowing rational control of not only protein folding, but also the design of pathways that lead to these folds,” says Shakhnovich, who has studied protein folding for nearly two decades.
As far back as 1981, it was pointed out that we don’t absolutely have to understand how natural proteins fold in order to design ones that fold the way we want, and that doing so is one pathway to a general ability to pattern matter with atomic precision. But it sure it ought to help! Kudos to the team. —Christine
