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. Author manuscript; available in PMC: 2010 Jul 21.
Published in final edited form as: Chem Biol. 2006 Dec;13(12):1297–1305. doi: 10.1016/j.chembiol.2006.10.006

Figure 2. Analysis of AgRP(83–132) 1H Chemical Shifts Derived from Both the Full-Length Protein and the Isolated C-Terminal Domain.

Figure 2

(A) The measured 1H chemical shifts from AgRP(83–132), minus the consensus random coil chemical shifts. The significant variation is consistent with a folded domain. Circles represent measured values; squares represent proline, which is not observable in the HSQC spectra. The arrows show the locations of β strands adjacent to the RFF triplet (residues 111–113).

(B) The difference in chemical shifts, full-length minus C-terminal, for residues 83–132. Note that the vertical axis is expanded by a factor of three compared to that in (A). The limited scatter demonstrates that the HSQC from residues 83–132 in full-length AgRP is essentially equivalent to that of the isolated C-terminal domain, AgRP(83–132). The 2 residues that do show significant 1H chemical shift variations are Arg89 and His91, as indicated.