Optical tweezers allow the detection of unfolding and refolding transitions in individual proteins, and how interacting molecules such as chaperones affect these transitions. Typical methods that tether individual proteins are based on cysteine chemistry, which is less suitable for proteins with essential cysteines. Here we describe a cysteine-independent tethering protocol that can be performed in situ.
CITATION STYLE
Moayed, F., van Wijk, R. J., Minde, D. P., & Tans, S. J. (2018). Protein tethering for folding studies. In Methods in Molecular Biology (Vol. 1665, pp. 43–51). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7271-5_3
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