TY - JOUR
T1 - Single-Molecule Rotation for EGFR Conformational Dynamics in Live Cells
AU - Park, Youngchan
AU - Shin, Sangwon
AU - Jin, Hyeonggyu
AU - Park, Jiseong
AU - Hong, Yeonki
AU - Choi, Jaemin
AU - Jung, Byunghyuck
AU - Song, Hyunjoon
AU - Seo, Daeha
N1 - Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/11/14
Y1 - 2018/11/14
N2 - Monitoring the dynamics of proteins in live cells on appropriate spatiotemporal scales may provide key information regarding long-standing questions in molecular and cellular regulatory mechanisms. However, tools capable of imaging the conformational changes over time have been elusive. Here, we present a single-molecule stroboscopic imaging probes by developing gyroscopic plasmonic nanoparticles, allowing for replication of protein-protein interactions and the conformational dynamics based on rotational and lateral velocities. This study fundamentally monitors the rotational motion of a membrane protein, epidermal growth factor receptor (EGFR), to decipher undiscovered structural dynamics in live cells without any molecular perturbations. This method offers a strategy to visualize assemblies and conformational changes, and provides unique insights into the mechanism underlying the molecular dynamics for receptors.
AB - Monitoring the dynamics of proteins in live cells on appropriate spatiotemporal scales may provide key information regarding long-standing questions in molecular and cellular regulatory mechanisms. However, tools capable of imaging the conformational changes over time have been elusive. Here, we present a single-molecule stroboscopic imaging probes by developing gyroscopic plasmonic nanoparticles, allowing for replication of protein-protein interactions and the conformational dynamics based on rotational and lateral velocities. This study fundamentally monitors the rotational motion of a membrane protein, epidermal growth factor receptor (EGFR), to decipher undiscovered structural dynamics in live cells without any molecular perturbations. This method offers a strategy to visualize assemblies and conformational changes, and provides unique insights into the mechanism underlying the molecular dynamics for receptors.
UR - https://www.scopus.com/pages/publications/85056406353
U2 - 10.1021/jacs.8b09037
DO - 10.1021/jacs.8b09037
M3 - Article
C2 - 30380855
AN - SCOPUS:85056406353
SN - 0002-7863
VL - 140
SP - 15161
EP - 15165
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 45
ER -