Figure 3.

The H^α secondary shifts of the N-terminal domain of IIA^Glc in a variety of detergents as a function of the residue number. The H^α secondary shift is defined as the chemical-shift difference between that of the peptide measured here and that in a random-coiled peptide ( Wüthrich 1986). Shown in A is the plot in SDS at a peptide:SDS molar ratio of 1:20, in B in DHPG at a peptide:DHPG ratio of 1:10, and in C in DSS at a peptide:DSS ratio of 1:40. The well-resolved shift for Gly1 was used in all cases.