Chromophore protonation state controls photoswitching of the fluoroprotein asFP595.

ABSTRACT: Fluorescent proteins have been widely used as genetically encodable fusion tags for biological imaging. Recently, a new class of fluorescent proteins was discovered that can be reversibly light-switched between a fluorescent and a non-fluorescent state. Such proteins can not only provide nanoscale resolution in far-field fluorescence optical microscopy much below the diffraction limit, but also hold promise for other nanotechnological applications, such as optical data storage. To systematically exploit the potential of such photoswitchable proteins and to enable rational improvements to their properties requires a detailed understanding of the molecular switching mechanism, which is currently unknown. Here, we have studied the photoswitching mechanism of the reversibly switchable fluoropr

SUBMITTER: Schafer LV 

PROVIDER: S-EPMC2274881 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature