a
Structural type of the transmembrane region, either
α-helical or
β-stranded
b
Including tagged or labeled derivatives of the basic structure
c
Includes THAM-based and glucose-based NAPols;
“NAPols,” otherwise, refers only to any of the various forms of glucose-based NAPols
d
A reproducible protocol could not be established for refolding BR by direct transfer from TFE to A8-35, but an artifactual result is highly improbable (see text)
e
OAPA-20 is almost identical to A8-75; PMAL-B-100 and PMAL-C12 are two different names for the same polymer (see Gorzelle et al. 2002 and Chap. 4)
f
The peptides, which are
α-helical in lipid bilayers, SDS, TFE, DMSO, and, presumably, in the native V-ATPase, adopted a
β-strand structure in A8-35, presumably due to a
mid-segment arginine interacting with the carboxylate groups of the APol
g
In Damian et al. (2012) and Casiraghi et al. (2016), the GPCR was folded in A8-35 and then transferred to nanodiscs for functional measurements; see
§ 5.7
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5 Formation and Properties of Membrane Protein/Amphipol Complexes