Abstract by Supeshala Dilrukshi Sarath Nawarathnage

Personal Infomation

Presenter's Name

Supeshala Dilrukshi Sarath Nawarathnage

Degree Level


Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

James Moody


Polymer driven protein crystallization chaperones


Atomic-level structures of proteins are essential for structure-function studies and structure-based drug design. X-ray crystallography is required for atomic level structure determination of proteins too small for cryo-electron microscopy and too large for nuclear magnetic resonance spectroscopy. Protein crystallization is the rate limiting step in protein structure determination using X-ray diffraction. Investigation of covalent and noncovalent protein crystallization chaperones to facilitate the crystallization of novel protein targets is important as it increases the success rate of protein crystallization. Polymerization of the chaperone-target protein fusion would lend avidity to strengthen subsequent weak crystal contacts made by the target protein. As the chaperone provides many of the crystal contacts, chaperones should enable protein crystallization with minimal screening of crystallization conditions, significantly reducing the time and resources required to determine protein structure. pH-sensitive TELSAM dimers that are redesigned to interconnect rigidly using coiled coils, drive the generation of 3D crystals.