Probing actin filament and binding protein interaction using an atomic force microscopy.

Actin filaments play essential roles in many kinds of cellular functions by interacting with hundreds of actin binding proteins. Here we probe the interaction between actin filament and a binding protein, α-actinin, using an atomic force microscopy (AFM) and dynamic force spectroscopy (DFS). The distribution of rupturing events including specific and non-specific interactions of actin filament/α- actinin and BSA/α-actinin were analyzed.

Real-time monitoring of changes in microtubule mechanical properties in response to microtubule-destabilizing drug treatment.

Microtubules are cylindrical protein polymers that play important roles in a number of cellular functions. The properties of microtubules are dynamically changed by interacting with many microtubule-related proteins and drugs. In this study, we used atomic force microscopy to evaluate the changes in microtubule mechanical properties induced by treatment with nocodazole, which is a microtubule-destabilizing drug.

Investigation of ubiquitin deformation mechanism under induced stretch-compression loads.

Proteins folding and unfolding are conformational changes in the life of the proteins, which reveal the modifications in the organization of the molecules inside the chain. It is known that a very organized structure has great amount of entropy and tends to exchange the energy with the environment. The present work presents the results of the atomistic modeling using NAMD software released by the University of Illinois, USA, to reveal the hyper-elasticity under external loads and the progressive conformational shapes that are produced by the H-bonds breaking and recovering.