Actin assembly analysis

Kang et al. recently used the KINSIM/FITSIM software to model barbed-end actin polymerization (See Actin Assembly Kinetics) in the absence and presence of profilin and/or thymosin-j84. This data analysis protocol permitted them to derive rate constants from a series of... 

In Section II, we will concentrate on characterizing smooth muscle actin and its isoforms, primarily from a biochemical perspective. In Section III, we will present our current understanding of the structure of native actin assemblies, that is, of thin filaments, which is based largely on analysis of electron microscope images. 

Analysis of Actin Assembly by In Vitro TIRF Microscopy... 

In thinking about X-ray diffraction from this assembly, a number of the sarcomere components contribute to the observed patterns in ways that have been the subject of detailed analysis. In the A-band, these include the myosin filament backbone, where the coiled-coil a-helical myosin rods pack together, the myosin head arrays in the bridge regions of the myosin filaments, the non-myosin A-band proteins titin and C-protein (MyBP-C), and the A-band parts of the actin filaments. Very little has been seen in X-ray patterns so far that appears to be related to the M-band, probably... 

Protein filaments. Here, we can use the example of the actin filaments and bundles to demonstrate the analysis of SAXS solution scattering. In Section 6.4.1, we introduced the filamentous protein F-actin and its self-assembly. The filaments will form networks or bundles of filaments under different solution conditions we can use fluorescence microscopy to observe these structures in the cell (Figure 6.18). F-actin is a negatively charged filament, and we can also think of it as a semiflexible, long, rod-like colloid when in solution. 

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