Abstract
A new hydrogen exchange method makes it possible to study the unfolded state of a protein and its partially unfolded forms under native conditions. The hydrogen bonded groups that are exposed in each state, identified by NMR-detected hydrogen exchange measurements, define the structure of each intermediate. The free energy level of each state can be obtained from the measured hydrogen exchange rates. Initial results with cytochrome c depict four structural units which together account for the entire protein structure. The intermediate forms reveal the cooperative substructure of the protein and appear to represent the major kinetic intermediates in the protein folding pathway.
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Bai, Y., Englander, S.W. (1996). The Cooperative Substructure of Protein Molecules. In: Jardetzky, O., Lefèvre, JF. (eds) Dynamics and the Problem of Recognition in Biological Macromolecules. NATO ASI Series, vol 288. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5839-2_1
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DOI: https://doi.org/10.1007/978-1-4615-5839-2_1
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