Min, Duyoung

Assistant Professor

Nano Bio Dynamics Laboratory

Lab: NSB (108) 810

Office: NSB (108) 801-10

E-mail: dymin@unist.ac.kr

Phone: +82-52-217-2675

Min, Duyoung

Assistant Professor

Nano Bio Dynamics Laboratory

E-mail: dymin@unist.ac.kr

Lab: NSB (108) 810

Office: NSB (108) 801-10

Phone: +82-52-217-2675

Research Areas

single-molecule force and fluorescence methods, membrane protein folding, protein-protein interaction, protein oxidation and damage, single-molecule enzyme kinetics, molecular dynamics simulation

Research Summary

We study membrane protein science at single-molecule resolution, hopefully contributing to pertinent areas of pharmacy and medicine. Proteins classified as membrane proteins are the key targets of commercial drugs (~60% of drugs), and thus better understanding of their hidden chemistry and physics cannot be more emphasized to develop effective strategies of therapeutic intervention. However, the progress is relatively slow due to the technical challenges in handling the recalcitrant membrane proteins. The vision of our laboratory is not only to understand their fundamental bio-physico-chemical principles such as misfolding disease mechanisms at single-molecule level, but also to develop new methods tackling the notorious.

Education

Ph.D., Biophysics, KAIST (2014)
B.S., Electrical Engineering, Hanyang University (2008)

Career

Assistant Professor, Department of Chemistry, UNIST (2019.10 ~ present)
Postdoctoral Fellow, Department of Chemistry & Biochemistry, UCLA (2015.3 ~ 2019.9)
Postdoctoral Fellow, Department of Physics, KAIST (2014.9 ~ 2015.2)

Selected Publications

Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins
S. Kim†, D. Lee†, W.C.B. Wijesinghe, and D. Min*
eLife 12:e85882 (2023)

Watching helical membrane proteins fold reveals a common N- to C-terminal folding pathway
H.-K. Choi†, D. Min† et al.
Science 366, 1150 (2019)

Unfolding of a ClC chloride transporter retains memory of its evolutionary history
D. Min et al.,
Nature Chemical Biology 14, 489 (2018)

Mapping the energy landscape for second-stage folding of a single membrane protein
D. Min et al.
Nature Chemical Biology 11, 981 (2015)

Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover
J.K. Ryu†, D. Min† et al.
Science 347, 1485 (2015)