Pheromone-binding proteins of lepidopteran moths (Antheraea polyphemus, Bombyx mori, Amyelois transitella etc.). The C-terminal tetradecapeptide of these proteins is a random coil in the ligand-bound form, and assumes a helical structure in the absence of ligand which occupies the binding cavity. These reversible conformational changes in the proteins are so large that the ligand bound and unbound forms exhibit totally different 2D-HSQC NMR spectra. Uma. -- Uma Katre Columbus, IN 47201
On Thursday, February 27, 2014 2:43 PM, "Keller, Jacob" <[email protected]> wrote: Dear Crystallographers, Does anyone know of good examples of large, reversible conformational changes occurring between ligand-free and -bound states? Could also be a non-relevant molecule binding, like sulfate or something inducing dubiously -relevant changes. I already know of the calmodulin and periplasmic binding protein families, but does anyone know of others out there? All the best, Jacob Keller ******************************************* Jacob Pearson Keller, PhD Looger Lab/HHMI Janelia Farms Research Campus 19700 Helix Dr, Ashburn, VA 20147 email: [email protected] *******************************************
