Secondary Structure Prediction of Protein Constructs Using Random Incremental Truncation and Vacuum-Ultraviolet CD Spectroscopy

摘要: A novel uracil-DNA degrading protein factor (termed UDE) was identified in Drosophila melanogaster with no significant structural and functional homology to other binding or processing factors. Determination of the 3D structure UDE is excepted provide key information on description molecular mechanism action catalysis, as well general uracil-recognition nuclease action. Towards this long-term aim, random library ESPRIT technology applied overcome problems identifying soluble expressing constructs given absence precise domain content arrangement. Nine were chosen decipher relationships. Vacuum ultraviolet circular dichroism (VUVCD) spectroscopy performed define secondary location within its truncated variants. The quantitative analysis demonstrated exclusive α-helical for full-length protein, which preserved constructs. Arrangement bundles segments suggested new boundaries differ from conserved motifs determined by sequence-based alignment homologues. Here we demonstrate that combination VUVCD provides a confirms are useful further detailed studies.