Issue Date: August 21, 2017 | Web Date: August 15, 2017
Structure of superlong, ice-binding protein reported
After a decade of persistent effort, researchers have obtained the first complete structure of a bacterial protein with one of the longest folded conformations of any known protein—600 nm in length.
The protein is expressed on the surface of a bacterium called Marinomonas primoryensis, which lives in waters in and around Antarctica. The biomolecule, a so-called adhesin protein named M. primoryensis ice-binding protein (MpIBP), latches onto the underside of ice shelves, a near-surface location where . . .
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- Chemical & Engineering News
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