Abstract
The presence of an early intermediate on the folding pathway of ribonuclease A has been demonstrated by a study of the exchange reaction between the backbone amide protons in the folding protein and solvent protons using rapid mixing techniques. A structural analysis of the intermediate by two-dimensional 1H-NMR is consistent with the framework model of protein folding in which stable secondary structure first forms the framework necessary for the subsequent formation of the complete tertiary structure.
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Udgaonkar, J., Baldwin, R. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature 335, 694–699 (1988). https://doi.org/10.1038/335694a0
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DOI: https://doi.org/10.1038/335694a0
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