Spotlights on Recent JACS Publications

摘要

The standard view that proteins tend to form well-packed； relatively static structures is yielding to a more flexible paradigm. A new twist on this shifting understanding of protein structure and function comes from a study by Chad Petit and colleagues (DOI: 10.1021/jacs.6bl2058). The researchers find that a typical globular protein can end in volume, like a puffer fish, while keeping the same overall shape. The volume expansion gives the protein more room to move, and a previous study has found that these changes in internal motions are the source of allostery, the transmission of information about protein interactions from the binding site to distant sites within the protein. This study demonstrates that allostery can arise from sources other than canonical structure changes. Moreover, the findings suggest that the definition of the native protein state as a tightly packed globule may need to be revised, allowing for looser proteins that swell and contract to perform their functions. This unexpected observation has broad implications for our understanding of protein allostery, which enables protein function regulations in the cellular environment. Erika Gebel Berg, Ph.D.