Noninvasive Protein Structural Flexibility Mapping by Bimodal Dynamic Force Microscopy

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 f...

Determination of protein structural flexibility by microsecond force spectroscopy.

Proteins are dynamic molecular machines having structural flexibility that allows conformational changes. Current methods for the determination of protein flexibility rely mainly on the measurement of thermal fluctuations and disorder in protein conformations and tend to be experimentally challenging. Moreover, they reflect atomic fluctuations on picosecond timescales, whereas the large conform...

Repulsive bimodal atomic force microscopy on polymers

Bimodal atomic force microscopy can provide high-resolution images of polymers. In the bimodal operation mode, two eigenmodes of the cantilever are driven simultaneously. When examining polymers, an effective mechanical contact is often required between the tip and the sample to obtain compositional contrast, so particular emphasis was placed on the repulsive regime of dynamic force microscopy....

Periodicity in bimodal atomic force microscopy

Force sensing and mapping by atomic force microscopy

Over the past 15 years, advances in the ¢eld of atomic force microscopy (AFM) have broadened its use from a high-resolution imaging instrument to a device capable of detecting and quantifying single molecular forces between surfaces in nearnative conditions. This article reviews developments in the force sensing ¢eld and focuses particularly on research that has seen the AFM utilised to produce...