Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion
 

Transient On- and Off-Pathway Protein Folding Intermediate States Characterized with NMR Relaxation Dispersion

The earliest events in the folding of a protein are in general poorly understood. We used NMR R(2) relaxation dispersion experiments to study transient local collapse events in the unfolded-state (U) conformational ensemble of apomyoglobin (apoMb). Local residual secondary structure (seen in regions corresponding to the A, D, E, and H helices of the folded protein) is largely unchanged over the pH range of 2.3-2.75, yet a significant pH-dependent increase in the conformational exchange...

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