Noninvasive protein structural flexibility mapping by bimodal dynamic force microscopy.

Mapping of the protein structural flexibility with sub-2-nm spatial resolution in liquid is achieved by combining bimodal excitation and frequency modulation force microscopy. The excitation of two cantilever eigenmodes in dynamic force microscopy enables the separation between topography and flexibility mapping. We have measured variations of the elastic modulus in a single antibody pentamer from 8 to 18 MPa when the probe is moved from the end of the protein arm to the central protrusion. Bimodal dynamic force microscopy enables us to perform the measurements under very small repulsive loads (30-40 pN).

Initial stages of the contact between a metallic tip and carbon nanotubes.

We present an experimental and theoretical study of the interaction between a tip and single-walled carbon nanotubes (SWCNT) lying on a SiO2 surface. Adhesion and jump-to-contact forces (JC) are measured in a high vacuum system for SWCNT with diameters (D) ranging from 1.4 to 4.5 nm; we find adhesion forces approximately 3.2 nN and JC forces approximately 2.4 nN. Simulations yield adhesion forces in agreement with experiment showing that for D approximately 1.4 nm half of this force is due to tip-SWCNT and tip-SiO2 van der Waals interactions.