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This type of measurement should provide a powerful test of theoretical models for the conformational fluctuations of macromolecules.
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Previous studies have shown that overall fluctuations of macromolecule are accountable by a few low frequency eigenvectors with large eigenvalues (Zhu et al., 2013).
The time-resolved anisotropy r(t) is described by three exponents [Eq. (21)]: (21) with the characteristic times for overall rotation (ρoverall), backbone fluctuations of the macromolecule (ρbackbone) and rotations around the linker (ρlinker), respectively, fractional initial anisotropy amplitudes r0,i.
In this state the strain can be as high as a few hundred percent and is associated with the conformational movements of macromolecules, the failure of fluctuation network nodes in some places and their formation in other less strained places.
Physical Biology of Macromolecules.
Figure 3: Adsorption-induced degradation of macromolecules.
Binding cooperativity, solvation, titration of macromolecules.
By far the largest portion of macromolecules are the proteins.
BCHM G6270 Nmr Spectroscopy of Macromolecules.
BCHM G6275 Diffraction Analysis of Macromolecules.
Binding, cooperativity, solvation, and titration of macromolecules.
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