Direct Measurement of the Thermodynamic Parameters of Amyloid Formation By Isothermal Titration Calorimetry

2006-02-10 14:49 下载量：712

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Background This paper was chosen for it’s technical novelty and the application area. Review. · Some classic protein biophysics used to address a very important and highly ‘fundable’ process, namely amyloidosis, which can be the cause of very common diseases. · ITC used to study a polymerisation process by titrating protein nucleation ‘seeds’ with monomeric protein · The protein understudy is immunologically important and can be found in monomeric form in the blood. It is only a problem once it starts to form fibrils. · DSC was employed for classical reasons i.e. protein unfolding. Amyloidosis is an areas where many classical protein unfolding people have found a good source of funding and applicability of protein biophysics. · CD was also used but in addition it is nice to see a calorimetric paper with Electron microscopy and classic ‘wet’ biochemistry. · ITC was used to obtain equilibrium thermodynamic data but also to measure the rates of polymerisation i.e. as a kinetic tool. The event was slow and accessible by ITC. · The DCp and DH of fibril formation were compared to that of the native, monomeric protein. The DCps were similar but the DHs were very different suggesting that the fibrils are more loosely packed and have a larger number of cavities than the native protein.

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大昌华嘉科学仪器

钻石会员 | 第24年

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