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• W2058274562 abstract "All possible protein folding intermediates exist in equilibrium with the native protein at native as well as non-native conditions, with occupation determined by their free energy level. The study of these forms can illuminate the fundamental principles of protein structure and folding. Hydrogen exchange methods can be used to detect and characterize these partially unfolded forms at native conditions and as a function of mild denaturant and temperature. This information illuminates the requirements that govern the ability of kinetic and equilibrium methods to study folding intermediates." @default.
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• W2058274562 date "1996-02-01" @default.
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• W2058274562 title "Future directions in folding: The multi-state nature of protein structure" @default.
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• W2058274562 doi "https://doi.org/10.1002/(sici)1097-0134(199602)24:2<145::aid-prot1>3.0.co;2-i" @default.
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