Figure 6.

Comparison of ALP107-273 NMR chemical shifts with those observed in random coil conformations. A) Difference of 13C Cα chemical shifts with random coil as a function of amino acid residue number. The random coil values were taken from the Biological Magnetic Resonance Data Bank http://www.bmrb.wisc.edu webcite. The average difference for 13C Cα chemical shifts in an α-helix is +3 and in a β sheet is -1.5 [39]. B) The difference in 13C Cβ chemical shift to random coil conformation. The average reference value is -1 in an α helix and +3 in a β sheet [39]. Based on this analysis ALP107-273 does not appear to contain sequential residues with typical α helix or β sheet conformations.

Klaavuniemi et al. BMC Cell Biology 2009 10:22   doi:10.1186/1471-2121-10-22
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