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I’ve recently started collaborating with Rustem Litvinov and John Weisel from Penn’s medical school. They write papers with excellent terminology:
The binding between an A-knob and an a-hole is relatively strong and is characterized by a yield force of about 125 to 130 pN when the applied load is increased at the rate of 400 pN/s.
They are interested in the origins of blood clot elasticity, self-assembly (see above), and fibrinolysis. They recently measured the elasticity of a single clot fiber using optical tweezers. The next logical step is to push the elasticity investigations to the single molecule level. This is a great molecule for these studies because its mechanics is relevant physiologically – soft clots don’t stop blood and stiff clots don’t break apart – and it has an interesting alpha helical coiled-coil segment. A coiled-coil from the muscle motor myosin II was recently studied in Matthias Rief’s group and seems to refold under tension much faster than any other protein studied in single molecule mechanical experiments so far. I’ll write more about the fascinating world of coiled-coils soon.
Microreview: Fluorescence Correlation Spectroscopy What's New: Judge of the jungle
Biocurious is written by Andre Brown and Philip Johnson, since 2005. Content of the weblog is licensed under a Creative Commons Attribution-Share Alike 3.0 License.
