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. Author manuscript; available in PMC: 2015 Oct 23.
Published in final edited form as: Solid State Nucl Magn Reson. 2014 Oct 29;70:1–14. doi: 10.1016/j.ssnmr.2014.10.003

Fig. 8.

Fig. 8

Left: The K24S28 region of LRAP is a highly sensitive structural region. This sensitivity can be observed in the 1D spectra which show multiple resonances for the 13C′ of K24 whose relative intensities change as a function of the conditions. Multiple resonances are only observed for this residue in the protein, further evidence of the structural uniqueness of this region. Right, top: The structural sensitivity is quantitatively shown with REDOR studies, with distances ranging from 4.2 Å for the unbound, lypohilized protein (the distance expected for an ideal helix), to 5.7 Å for the bound, unphosphorylated protein, a very extended or random coil structure. Bottom, right: Other conditions such as the Ca2+ concentration when binding, or binding to carbonated HAP instead of HAP, also influence the structure. Reproduced with permission from Ref. [55] and Ref. [56], Copyright 2013 American Chemical Society.