Abstract by Moriah Longhurst
Supeshala Sarath Nawarathnage
Chemistry and Biochemistry
Polymer-Forming Protein Crystallization Chaperones
Identifying detailed protein structures is essential to understanding protein function. Protein crystallization, a technique used to determine the 3D structures of proteins by X-ray diffraction, is currently time consuming, expensive, and has a low success rate (10—30%). Attempts to improve this success rate have used crystallization chaperones, which help the target proteins align and crystallize. Our goal is to develop a new technique that will be widely used to crystallize proteins, resulting in easier and more frequent successful crystallization and structure determination.
Nauli et al. fused eleven proteins to a pH sensitive protein polymer called 2TEL, composed of two TELSAM subunits, and all of these proteins crystallized successfully. However, most gave crystals that were too disordered to provide useful data.
We hypothesize that utilizing the TELSAM domains 1TEL, 2TEL, and 3TEL, and 1TEL-VFL could lead to crystallization of challenging proteins. CMG2, our target protein, has proven difficult to crystallize on its own, so successful crystallization using this technique would demonstrate the efficacy of TELSAM polymers as chaperones.