Home > Press > Computer-rendered flexibility map of Bacteriorhodposin
Nanomechanical Sensing Group, Rowland Institute at Harvard |
Abstract:
Investigators study the properties of proteins, akin to tiny molecular machines with complex moving parts, by analyzing their crystal structures.
Given the extremely small physical dimensions involved, capturing the "frozen images of their atoms" is extremely difficult. Moreover, these molecular machines work fast---moving to and fro in mere microseconds. To take a snapshot, a team at the Rowland Institute at Harvard led by Ozgur Sahin, Primary Investigator and Junior Fellow, and Sudhir Husale, postdoctoral fellow, developed a new technology called microsecond force spectroscopy. The method offers dramatically improved spatial and temporal resolutions in mechanical measurements and provides researchers with a robust platform to investigate a wide range of proteins involved in diseases and other biological processes. Pictured is a computer-rendered flexibility map of Bacteriorhodposin, a membrane protein that converts light into electrical energy. The findings were published online in Nature on December 13. Sahin and Husale's collaborators included Henrik H. J. Persson, a Research Associate at the Stanford Genome Technology Center, and Mingdong Dong, a postdoctoral fellow at Rowland.
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