Xinyi Zhang


Xinyi Zhang, a Chemistry third-year graduate student currently supported by the NSF KY EPSCoR (Membrane Pillar) program, was born in China. Her Research Advisor is Dr. Yinan Wei. She became interested in science/research after her biology teacher in China “made the class funny”, as she recalls, forming her interest in science. Subsequently, as a student in China with exceptional GPA, she recognized she could have above average opportunities to go to a college of her choice. She wanted to further her education in the USA because of more opportunities and research facilities that would be available to her. The University of Kentucky offered a Teaching Assistant Fellowship in conjunction to further her research for her Ph.D. and she accepted the offer.
            Because of her curiosity of wanting to know why and how,-what-and-why she began to realized research would explain the steps and bring solutions with a clear explanation of a begin-point and an end-point.
Xinyi explains her research as follows: Membranes define the boundary of life. Cell membrane protects and separates the interior of the cell from the environment. The major components of cell membranes are a phospholipid bilayer and a diverse array of membrane proteins. Membrane proteins play important roles in biological processes including signal transduction, selective import and export of materials, catalysis, and energy production. To exploit the diverse functions of natural membrane proteins, biomimetic membranes(jointly with Prof. Bhattacharyya and his group) are created to incorporate membrane proteins in an artificial supporting matrix. However, there are few challenges in constructing biomimetic membranes, including maintaining the membrane protein stability and incorporating the protein into the membrane. My research focuses on the development and application of novel methods to incorporate membrane proteins into biomimetic membranes.  Since the selectivity of the membrane requires the membrane protein to function in a specific direction, we are working to design and validate several novel approaches to enable directional immobilization of membrane proteins. In parallel, we are working on the coupling of protein biosynthesis with insertion into size-controlled lipid bilayer nanodiscs. This cell free procedure eliminates the membrane extraction step during protein purification, which is especially useful for membrane proteins that are readily denatured during membrane extraction.

She was recognized at the Kentucky Academy of Science meeting in November, 2014 and placed 2nd in the oral’s competition.

Xinyi is preparing now to present a poster identifying her research in the May, 2015 25th Annual NAMS Meeting in Boston, MA.

Wang Z, Ye C, Zhang X, Wei Y. Cysteine residue is not essential for CPM protein thermal-stability assay. Anal Bioanal Chem, in PRESS (Mar 14, 2015).

Gajadeera CS, Zhang X, Wei Y, Tsodikov OV. Structure of inorganic pyrophosphatase from Staphylococcus aureus reveals conformational flexibility of the active site. J Struct Biol.189(2):81-6 (2015).

 Chai Q, Ferrell B, Zhong M, Zhang X, Ye C, Wei Y. Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA. Protein Eng Des Sel. 27(4):111-6 (2014).