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. 2008 Oct 3;95(12):5951–5961. doi: 10.1529/biophysj.108.139899

FIGURE 1.

FIGURE 1

Myoglobin conformation in amorphous solids containing various additives (1:1 w/w). (A) Second derivative FTIR spectra. (B) ssHDX of intact protein. (C) ssHDX of peptic digests. Additives were trehalose (Tre), raffinose (Raf), dextran (dex), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), and guanidine hydrochloride (Gdn). In C, peptic fragments and approximate secondary structures were: 1 (G1-W7; 42% α-helix), 2 (Q8-L11; 100% α-helix), 3 (N12-A19; 67% α-helix, 33% turn), 4 (I21-L29, 100% α-helix), 5 (I30-L40, 100% α-helix), 6 (G35-L40, 100% α-helix), 7 (M55-L69, 100% α-helix), 8 (T70-L76, 100% α-helix), 9 (G80-L86, 71% α-helix), 10 (K87-Y103, 47% α-helix), 11 (A110-D126, 52% α-helix, 17% turn), 12 (I142-K147, 100% α-helix), and 13 (L149-G153, 20% α-helix). In B, asterisk indicates significant difference from the value for the “None” sample (α = 0.05); n = 3 ± SD.