Abstract
By using high-speed and high-resolution Atomic Force Microscopy (AFM), it was possible to resolve within a single experiment the kinetic pathway in S-layer self-assembly at the solid-liquid interface, obtaining a model that accounts for the nucleation, growth and structural rearrangements in 2D protein self assembly across time (second to hours) and spatial scales (nm to microns).
Cite
CITATION STYLE
APA
Stel, B., Cometto, F., Rad, B., De Yoreo, J. J., & Lingenfelder, M. (2018). Dynamically resolved self-assembly of S-layer proteins on solid surfaces. Chemical Communications, 54(73), 10264–10267. https://doi.org/10.1039/C8CC04597F
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