Home > Press > Computer-rendered flexibility map of Bacteriorhodposin
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| 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.
Computer-rendered flexibility map of Bacteriorhodposin
Cambridge, MA | Posted on January 12th, 2010
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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