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  • Title: Formation of the hydrophobic core of ribonuclease A through sequential coordinated conformational transitions.
    Author: Navon A, Ittah V, Scheraga HA, Haas E.
    Journal: Biochemistry; 2002 Dec 03; 41(48):14225-31. PubMed ID: 12450386.
    Abstract:
    With steady-state and time-resolved fluorescence energy-transfer measurements, we determined the distributions of intramolecular distances in nine mutants to study the conformations of wild-type ribonuclease A in the reduced state under folding conditions. Although far-UV-CD measurements show no evidence for a secondary-structure transition, temperature- and GdnHCl-induced changes in intramolecular distance distributions in the reduced state revealed evidence for long-range subdomain structures in the denatured protein. These poorly defined structures, reflected here by wide distributions corresponding to a wide range of energies, form during refolding in a complex sequence of multiple subdomain transitions. A more well-defined structure emerges only when this structural framework, which directs the successive steps in the folding process, matures and is reinforced by stronger interactions such as disulfide bonds.
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