Metastability of native proteins and the phenomenon of amyloid formation
Journal of the American Chemical Society, 2011•ACS Publications
An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils
reveals that this structural form is likely to be the most stable one that protein molecules can
adopt even under physiological conditions. This result challenges the conventional
assumption that functional forms of proteins correspond to the global minima in their free
energy surfaces and suggests that living systems are conformationally as well as chemically
metastable.
reveals that this structural form is likely to be the most stable one that protein molecules can
adopt even under physiological conditions. This result challenges the conventional
assumption that functional forms of proteins correspond to the global minima in their free
energy surfaces and suggests that living systems are conformationally as well as chemically
metastable.
An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable.
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