Abstract
Amyloid fibril deposition is associated with over 20 degenerative human diseases, including Alzheimer's, Parkinson's, and prion diseases. Although research over the last few years has revealed the morphology and structural features of amyloid fibrils, knowledge about the thermodynamics of amyloid fibril formation and its thermal unfolding is limited. First, we describe the thermodynamic studies of β2 microglobulin amyloid formation by means of isothermal titration calorimeter. Then, we outline the unique thermal response of its mature amyloid fibrils in comparison with the thermal unfolding of the native form.
