Journal of the American Chemical Society · 2011 · 435 citations · 21 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryProtein FoldingStructural BiologyAmyloid FormationBiomolecular ThermodynamicsBiophysical ThermodynamicsProtein ConformationProtein DynamicsProtein StructureAmyloid Fibril FormationAmyloid Fibril StructureAmyloid FibrillogenesisAmyloid FibrilsAmyloid StructureFree Energy SurfacesLocal Energy MinimaProtofibril Formation
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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Initial sequencing and analysis of the human genome
Eric S. Lander, Lauren Linton, Bruce W. Birren et al. · Nature · 2001 · 24.6K citations · Full text