This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The goal of our research is to study the cotranslational folding of apomyoglobin at high resolution via fluorescence anisotropy and fluorescence resonance energy transfer (FRET). We have focused our studies on a series of ribosome-bound proteins chains stalled at varying points during translation. The site-specific incorporation of a single fluorphore, will allow the study the anisotropic motions of the fluorophore and will elucidate the environment and the compaction of the protein as a function of chain length. The introduction of a second site-specific fluorophore will allow for the measurement of distance-dependent energy transfer between the fluorophores; these distances will illuminate the changing protein structure as it elongates. The powerful combination of these biophysical and chemical tools will provide a clear and necessary model of cotranslational protein folding as well as a series of methods for future, more targeted explorations of misfolded proteins.
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