Rotational dynamics and transition mechanisms of surface-adsorbed proteins.

ABSTRACT: Assembly of biomolecules at solid–water interfaces requires molecules to traverse complex orientation-dependent energy landscapes through processes that are poorly understood, largely due to the dearth of in situ single-molecule measurements and statistical analyses of the rotational dynamics that define directional selection. Emerging capabilities in high-speed atomic force microscopy and machine learning have allowed us to directly determine the orientational energy landscape and observe and quantify the rotational dynamics for protein nanorods on the surface of muscovite mica under a variety of conditions. Comparisons with kinetic Monte Carlo simulations show that the transition rates between adjacent orientation-specific energetic minima can largely be understood through traditional mo

SUBMITTER: Zhang S 

PROVIDER: S-EPMC9169768 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature