| Range |
0.25 nm
|
| 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.227 right column 2nd paragraphPubMed 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 right column 2nd paragraph: "The unfolding distance (Δxu) is identical to that of the wild-type protein, 0.25 nm (primary source), which indicates that the engineered disulfide bond has not altered the distance to the transition state. However, the spontaneous unfolding rate constant is increased 5.6 times, suggesting a reduced stability of the mutant protein." |
| Entered by |
Uri M |
| ID |
114334 |