Skip to main content
. 2020 Jun 5;25(11):2634. doi: 10.3390/molecules25112634

Table 1.

47-mer peptides as the sequential models of the Gly-rich region in Figure 3 as underlined sequence, a flanked by (Ala)6 at both ends [46,60,62]. (I) The peptides, 2–7 were used for determinations of both the inter-nuclear distances of 15N and 13C labeled sites, and the fractions of the local conformations of 13C labeled Gly residues. (II) The peptides, 8–10 were used for determination of the fractions of the local conformations of the 13C labeled Gly-Ala-Gly motifs.

I: REDOR and 13C CP/MAS NMR Experiments Distance *
1 (E)4(A)6GGAGQGGYGGLGSQGAGRGGLGGQGAG(A)6(E)4
2 (E)4(A)6GGA[1-13C]G14Q[15N]G15GYGGLGSQGAGRGGLGGQGAG(A)6(E)4 3.71 Å
3 (E)4(A)6GGAGQG[1-13C]G17Y[15N]G19GLGSQGAGRGGLGGQGAG(A)6(E)4 3.97 Å
4 (E)4(A)6GGAGQGGYG[1-13C]G20L[15N]G22SQGAGRGGLGGQGAG(A)6(E)4 3.41 Å
5 (E)4(A)6GGAGQGGYGGLGSQGA[1-13C]G27R[15N]G29GLGGQGAG(A)6(E)4 3.64 Å
6 (E)4(A)6GGAGQGGYGGLGSQGAGRG[1-13C]G30L[15N]G32GQGAG(A)6(E)4 3.43 Å
7 (E)4(A)6GGAGQGGYGGLGSQGAGRGGLG[1-13C]G33Q[15N]35GAG(A)6(E)4 3.81 Å
II: 13 C CP/MAS NMR Experiment
8 (E)4(A)6G [2-13C]G12 [3-13C]A13 [1-13C]G14QGGYGGLGSQGAGRGGLGGQGAG(A)6(E)4
9 (E)4(A)6GGAGQGGYGGLGSQ [2-13C]G25 [3-13C]A26 [1-13C]G27RGGLGGQGAG(A)6(E)4
10 (E)4(A)6GGAGQGGYGGLGSQGAGRGGLGGQ [2-13C]G35 [3-13C]A36 [1-13C]G37(A)6(E)4

Distance * is the inter-nuclear distance between 15N and 13C labeled sites [46].