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Minh DoanProbing the Folded State of Fibronectin Type III Domains in Stretched Fibrils by Measuring Buried Cysteine Accessibility The Journal of Biological ChemistryChristopher A. Lemmon, Tomoo Ohashi, and Harold P. EricksonUnder mechanical load, fibronectin unfolds, resulting in exposure of cysteine residues. These mechanical forces can disrupt hydrogen bonding and van der waals interactions that contribute to the cell’s folded state. If fibronectin unfolded, then it would have more residues exposed in the extracellular space. Therefore, we could see what proteins bind to specific cysteine residues and how they affect cell activity. Ultimately, the conformation of the cell changes what molecules can bind to it and the overall activity of the cell. In addition, unfolding of fibronectin allows it to be stretched into fibrils that bond with one another that allows greater elastic properties and increases its ability to withstand mechanical stress.The study labelled cysteine residues to evaluate the folded state of FN-III in fibronectin. Cysteine labeling uses thiol reactive dyes to determine if cysteine amino acids are exposed or