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Abstract
Biteen studies gut bacterial communities at the University of Michigan in Ann Arbor, and was eager to use fluorescent proteins to identify individual species in complex mixtures. A relatively new addition to the fluorescent-protein palette, IFP2.0 fluoresces mainly in the near-infrared - a portion of the electromagnetic spectrum that is barely visible to the human eye but readily apparent to microscope cameras1. Another is to engineer natural far-red and near-infrared proteins so that they work better outside their usual host, for example by boosting the efficiency of the binding between the protein and the pigment, says Vladislav Verkhusha, a molecular bioengineer at Albert Einstein College of Medicine in New York City. Timothy Wannier, a synthetic biologist at Harvard Medical School, used both molecular evolution and computer-based protein analysis and design on GFP relatives during his PhD studies at the California Institute of Technology in Pasadena.