Abstract
Filamin A is an important cytoskelton crosslinking protein containing 24 immunogloble domains. Force spectroscopy of Filamin A has been studied by AFM. We use a new technology to study the response of Fimalin A to stretching force. When we apply a constant force ∼50 pN to unfold a construct that is composed of 1-8 domains, distinct and nearly equal unfolding steps are observed (Fig. 1). When decreasing force to ∼5 pN, refolding events of several previously unfolded domains is observed (Fig. 2). At the same time, from the force extension curve of unfolded proteins, the persistence length of polypeptide is estimated to be ∼0.6 nm.
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