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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Oct 21;1808(1):498–507. doi: 10.1016/j.bbamem.2010.10.011

Figure 7. CαH proton chemical shifts indicate predominantly α helical secondary structure of [113-122]apoJ in the presence of DPC micelle.

Figure 7

A plot of the ΔδCαH (δobserved-δcoil) chemical shift for all the residues in [113-122]apoJ. Note that the CαH protons show an upfield shift compared to the corresponding coil values, indicating α-helical structure. Random coil chemical shifts used were those reported in: Wuthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, Inc., New York