| Range |
contour length 28.4±0.3nm: unfolding force 204±26
|
| Organism |
Human Homo sapiens |
| Reference |
Ainavarapu SR et al., Contour length and refolding rate of a small protein controlled by engineered disulfide bonds. Biophys J. 2007 Jan 1 92(1):225-33 p.228 table 1PubMed ID17028145
|
| Primary Source |
[13] M. Carrion-Vazquez et al., Mechanical and chemical unfolding of a single protein: a comparison Proc. Natl. Acad. Sci. USA, 96 (1999), pp. 3694-3699PubMed ID10097099
|
| Method |
Atomic force microscopy (AFM) |
| Comments |
P.227 left column bottom paragraph: "The characteristics of each construct in terms of the number of unsequestered amino acids, the number of trapped amino acids, their respective contour lengths, and force distributions are presented in Table 1. Fig. 2, B and C, shows histograms of the contour length increments measured from all four constructs (ΔLu in Fig. 2 B and ΔLr in Fig. 2 C). In all four cases, the sums of ΔLu + ΔLr (∼28.8 nm) are within the error of the contour length measured for the fully reduced proteins (∼28.4 nm), where the disulfide bond is reduced before mechanical stretching (Table 1)." |
| Entered by |
Uri M |
| ID |
114333 |