Protein Folding Intermediates: Native-State Hydrogen Exchange

• DOI: 10.1126/science.7618079
• Publication Date: 2006-10-27T18:19:42Z
• Authors: Yawen Bai; Tobin R. Sosnick; Leland Mayne; S. Walter Englander
• Keywords: Metastability; Folding (DSP implementation); Sequence (biology); Intermediate state

The hydrogen exchange behavior of native cytochrome c in low concentrations denaturant reveals a sequence metastable, partially unfolded forms that occupy free energy levels reaching up to the fully state. step from one form another is accomplished by unfolding or more cooperative units structure. are entire omega loops mutually stabilizing pairs whole helices and loops. detected appear represent major intermediates reversible, dynamic reactions occur even at conditions thus may define pathway for folding.