Monday, October 17, 2011: 10:10 AM
L100 F (Minneapolis Convention Center)
The extracellular matrix protein fibronectin plays critical roles during cancer progression, wound repair, and cell differentiation. A variety of evidence suggests that fibronectin experiences mechanical stretch as part of its physiological function, and that this stretch may lead to partial unfolding of individual fibronectin domains. In this study, we exert mechanical load on single fibronectin molecules using magnetic tweezers, and observe the resulting conformational changes in domain unfolding using a 3D particle tracking algorithm capable of nanometer resolution. Ongoing studies using these techniques examine the complex conformational dynamics of native fibronectin and its binding partners.