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. Author manuscript; available in PMC: 2019 Jun 21.
Published in final edited form as: J Phys Chem B. 2018 Mar 6;122(10):2725–2736. doi: 10.1021/acs.jpcb.7b11596

Figure 2.

Figure 2.

NMR spectral assignments of designed elastin proteins 2 and 4 and their component domains. 15N HSQC peaks from the isolated hydrophobic module, 24’ (blue), and cross-linker, X’ (red), are superimposed on spectra (black peaks) of minielastins 2 (left) and 4 (right) that contain them. Assignments indicate the module and the residue position within the module. For example, A1,24 is the first residue in the APGVGV repeat of the 24’ hydrophobic module and A4,X or A4,X’ are the fourth residues in the 2123 or X’ cross-link modules, respectively.