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. 2012 May 22;287(31):26178–26186. doi: 10.1074/jbc.M111.325555

TABLE 2.

Best fit values of the order parameter (S), helix tilt angle (τ), and the fraction of aggregated nonreconstituted peptide obtained by solid-state NMR analysis of PDGFRβ-TM in different bilayers

Peptide Thickness τ Aggregated S r.m.s.d.a
DLPC 20.9 Å NDb >0.70 0.98 0.00031
DMPC 25.4 Å 31° 0.54 0.94 0.00030
POPC 27.1 Å 17° 0.26 1.00 0.00024
DEPC 31.5Å 10° 0.04 0.98 0.00020

a Root mean square deviation.

b Due to the low fraction of oriented peptide, a meaningful result for the tilt angle was not obtained.