After compression to the desired surface pressure, the protein films were transferred to freshly cleaved mica that was rinsed with ethanol and briefly blow‐dried with pressurized air directly before transfer by using a Filmlift FL‐1 (MGW Lauda). Lifting occurred with an approach speed of 25 cm min−1. After 24 s of contact with the interface, the substrate was lifted with a speed of 30 cm min−1. The samples were dried in a desiccator for 48 h, then measured at RT by using a Multimode AFM (Veeco Metrology) equipped with Tapping Mode cantilevers (BudgetSensors) with a spring constant of 5 N m−1, a nominal resonance frequency of 150 kHz, and a radius of <10 nm.
Images were recorded by using NanoScope (v. 7.30, Veeco) software and processed by using Gwyddion 2.49 (freeware;http://gwyddion.net ).
On average, three scans were recorded over the same area at a scanning rate of 0.5 Hz with a ratio of set‐point amplitude to free amplitude of ≈0.8. Results are reproducible because similar structures were recorded over four different areas on average per sample. Height and phase images were recorded simultaneously.
Images were recorded by using NanoScope (v. 7.30, Veeco) software and processed by using Gwyddion 2.49 (freeware;
On average, three scans were recorded over the same area at a scanning rate of 0.5 Hz with a ratio of set‐point amplitude to free amplitude of ≈0.8. Results are reproducible because similar structures were recorded over four different areas on average per sample. Height and phase images were recorded simultaneously.