Protein folding intermediates: native-state hydrogen exchange.
The hydrogen exchange behavior of native cytochrome c in low concentrations of denaturant reveals a sequence of metastable, partially unfolded forms that occupy free energy levels reaching up to the fully unfolded state. The step from one form to another is accomplished by the unfolding of one or more cooperative units of structure. The cooperative units are entire omega loops or mutually stabilizing pairs of whole helices and loops. The partially unfolded forms detected by hydrogen exchange appear to represent the major intermediates in the reversible, dynamic unfolding reactions that occur even at native conditions and thus may define the major pathway for cytochrome c folding.
Bai
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Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104-6059, USA.
Sosnick
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Mayne
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Englander
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D003574:Cytochrome c Group / Q000737:chemistry*; D019791:Guanidine; D006146:Guanidines / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry*; D006860:Hydrogen Bonding; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature; D013816:Thermodynamics
D003574:Cytochrome c Group; D006146:Guanidines; D006859:Hydrogen; D019791:Guanidine