||Stahl SW et al., Single-molecule dissection of the high-affinity cohesin-dockerin complex. Proc Natl Acad Sci U S A. 2012 Dec 11 109(50):20431-6. doi: 10.1073/pnas.1211929109 p.20433 left column 3rd paragraphPubMed ID23188794
|| Rief M, Gautel M, Schemmel A, Gaub HE (1998) The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys J 75(6):3008–3014 DOI: 10.1016/S0006-3495(98)77741-0PubMed ID9826620
||Atomic force microscopy
||P.20433 left column 3rd paragraph: "To measure the contour lengths of the various protein domains, the force–distance data were transformed into contour length space using a worm-like chain (WLC) model (ref 20). [Investigators] assumed a fixed persistence length of 0.4 nm, which was previously found to be appropriate for modeling protein unfolding in a high force (>50 pN) regime (primary source). After WLC transformation, cross-correlation (ref 22) of the data traces was performed to align the traces and correct for the polydispersity of the PEG [Polyethylene glycol] spacers. The transformed data traces were then combined to produce a barrier position histogram that exhibited characteristic contour length increments. This data transformation and analysis process is depicted in Fig. S3."