New insights may guide design of light-sensitive proteins with desired properties

New insights may guide design of light-sensitive proteins with desired properties

A team of scientists from the Department of Energy's SLAC National Accelerator Laboratory and Stanford University has gained insight into how electric fields affect the way energy from light drives molecular motion and transformation in a protein commonly used in biological imaging. A better understanding of this phenomenon, which is crucial to many processes that occur in biological systems and materials, could enable researchers to finely tune a system's properties to harness these effects, for instance using light to control neurons in the brain. Their findings were published in Science in January. Twist and shout Human vision, photosynthesis and other natural processes harvest light with proteins that contain molecules known as chromophores, many of which twist when light hits them. The hallmark of this twisting motion, called photoisomerization, is that part of the molecule rotates around a particular chemical bond. Something about the protein environment is steering this very specific and important process. One possibility is that the distribution of atoms in the molecular space blocks or allows rotation about each chemical bond, known as the steric effect. An alternative has to do with the idea that when molecules with double bonds are excited, there is a separation of charge, and so the surrounding electric fields might favor the rotation of one bond over another. This is called the electrostatic effect." Steven Boxer, a biophysical chemist and Stanford professor who oversaw the research A different tune To find out more about this process, the researchers looked at green fluorescent protein, a protein frequently used in biological imaging whose chromophore can respond to light in a number of ways that are sensitive to its local environment within the protein, producing fluorescent light of various colors and intensities. Stanford graduate students Matt Romei and Chi-Yun Lin, who led the study, tuned the electronic properties of the chromophore within the protein by introducing chemical groups that systematically added or subtracted electrons from the chromophore to engineer an electric field effect. Then they measured how this affected the chromophore's twisting motion. Related Stories



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