Research Interests
Our lab is mainly interested in protein/peptide structure, folding, and design. We use synthetic peptide models to study the folding problems of protein structures, including collagen, polyproline, α-helix and β-hairpin. The current research subjects include:
The folding and assembly of collagen-mimetic peptides: collagen is the most abundant protein in animals and folds into a triple helix consisting of three polyproline type II (PPII) helices. Each collagen strand is composed of approximately 300 repeats of the sequence: X-Y-Gly. Mutations of the glycine residue cause collagen abnormality and are associated with many diseases.
Design of collagen-mimetic peptides for heterotrimeric folds
Self-assembly of collagen mimics for potential biomaterials
Study of mutation effects on collagen
Functionalized peptides for metal sensors and catalysts
Based on small peptide motifs, such as β-hairpins, we incorporate specific amino acids in the sequence for the metal sensors with high selectivity and sensitivity
Using various peptide scaffolds, such as polyproline, α-helices, and β-sheets, to design catalysts
Folding study of protein and peptide structures
Stereoelectronic effects on polyproline conformation
The interactions involved in the stabilization of polyproline conformation conversion
Using proline derivates small peptide models to investiagte how proline puckers affect protein stability
Essentially, our research involves in biochemistry, protein chemistry, physical chemistry, biophysics, and structural biology, and thus the interdisciplinary knowledge and techniques can be learned for further exploring the world beyond chemistry.