Identification of Partially Disordered Peptide Intermediates through Residue-Specific NMR Diffusion Measurements

摘要

It is technically challenging to detect the low population of partially disordered species that are in equilibrium with the folded and unfolded states.Characterization of these states is critical to understand protein-folding processes and equilibrium properties.The ability of NMR to probe the exchange dynamics of intercon-verting species of proteins at specific residues allows the design of sophisticated experiments to approach the identification of these intermediates.Recently,relaxation dispersion NMR was used to define folding intermediates in equilibrium with its unfolded and fully folded states for an SH3 domain.