Correlation Force Spectroscopy for Single Molecule by Milad Radiom

By Milad Radiom

This thesis addresses the advance of a brand new strength spectroscopy device, correlation strength spectroscopy (CFS) for the dimension of the houses of very small volumes of fabric (molecular to µm3) at kHz-MHz frequency diversity. CFS measures the simultaneous thermal fluctuations of 2 closely-spaced atomic strength microscopy (AFM) cantilevers. CFS then calculates the cross-correlation within the thermal fluctuations that offers the mechanical houses of the problem that spans the space of the 2 cantilevers. The publication additionally discusses improvement of CFS, its merits over AFM, and its program in unmarried molecule strength spectroscopy and micro-rheology.

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5). 4) relates the autocorrelation of stochastic fluctuations of a single cantilever, x1 ( 0 ) x1 ( t ) , to its deterministic ringdown, X1 (t ) , after removal of a step force, F1, at time zero. t is the time and x is the deflection, which changes with time due to fluctuations. 4) is the fluctuation–dissipation theory for a single cantilever. 5) relates the cross-correlation of stochastic fluctuations between the two cantilevers, x1 ( 0 ) x2 ( t ) , to the deterministic response of the bottom cantilever, X 2 (t ) , as a result of ringdown of the top cantilever after removal of a step force F1, Analysis of Thermal Fluctuations to obtain Correlations  19 at time zero.

The frequency space comparison (between the power Limitations of AFM-Based SMFS  7 spectral densities) is shown earlier in this thesis since it is important to show that at all frequencies around the fundamental resonance frequency of the cantilevers, the noise is much smaller when the thermal motions of two cantilevers are correlated. After tethering a molecule between the two tips, there is a larger percentage of variation in the cross-correlation compared to the autocorrelation, giving a better force sensitivity.

Using the coarse-grained theoretical framework of Rouse with internal friction (RIF) model (see the section “Rouse with Internal Friction”), they studied the effect of solvent viscosity, segment length, and sequence composition on the internal friction of proteins. Their results suggest that the origin of internal friction is interaction between amino acid residues that are only partially exposed to solvent. Liu et al. [64] used laser temperature-jump relaxation experiment to study the effect of temperature on roughness of energy landscape during folding of protein FiP35.

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