Table 8.1
Studies relevant to the optical spectroscopy of amphipols and amphipol-trapped membrane proteins. Studies in which only static absorbance data are shown are not
listed, or studies relying only on light scattering (see Chap. 9) or on surface plasmon resonance measurements (see Chap. 13).
Study Protein
Amphipol
CD/
SRCD Fluorescence
RRS/
SERS TRAS Comments
References
8.1
Nicotinic acetylcholine
receptor (nAChR) from
Torpedo marmorata
A8-35
●
Comparative stopped-flow
studies of the binding of a
fluorescent agonist to the
nAChR in native membranes,
in detergent solution, or after
trapping by A8-35
Martinez et al. (2002)
8.2
Rabbit sarcoplasmic Ca
2+
-
ATPase (SERCA1a)
A8-35, SAPol, PMALC12, PMALA-C12
●
Kinetics of dissociation of Ca
2+
from the detergent-solubilized
or APol-trapped ATPase
Picard et al. (2006)
8.3
Bacteriorhodopsin
(BR) from Halobacterium
salinarum
A8-35, NAPols
●
Time-resolved absorbance
spectroscopy (TRAS) studies
of the photocycle of BR either
in its native state (in purple
membrane, detergent, or APols)
or after refolding in either the
presence or absence of lipids,
and either free in solution or
immobilized onto a solid
support
Pocanschi et al. (2006),
Gohon et al. (2008),
Charvolin et al. (2009),
Bazzacco et al. (2012), and
Dahmane et al. (2013)
8.4
OmpA from Escherichia
coli
and FomA from
Fusobacterium nucleatum
A8-35
●
Assessment of refolding
following transfer from urea to
A8-35
Pocanschi et al. (2006, 2013)
8.5
Transmembrane domain
(tOmpA) of E. coli
OmpA
A8-35, FAPol
NBD
●
Förster resonance energy
transfer (FRET) studies of the
exchange of FAPol
NBD for
unlabeled A8-35 or detergent at
the surface of tOmpA
Zoonens et al. (2007) and
Tribet et al. (2009)
8.6
Transmembrane peptides
from subunit a
of the
V-ATPase from
Saccharomyces cerevisiae
A8-35
●
●
CD and intrinsic
fluorescence
studies of the transfer of
transmembrane peptides from
trifluoroethanol to A8-35
Duarte et al. (2008)
8.7
LTB1, LTB2, CB1, and
5-HT
4(a) G protein-coupled
receptors (GPCRs)
A8-35
●
Fluorescence-based titration
assays of ligand binding to
GPCRs folded in A8-35
Dahmane et al. (2009),
Catoire et al. (2010), and
Mary et al. (2014)
(continued)
8.2 Optical Spectroscopy Studies of Amphipols and Membrane Protein/Amphipol Complexes
383
Studies relevant to the optical spectroscopy of amphipols and amphipol-trapped membrane proteins. Studies in which only static absorbance data are shown are not
listed, or studies relying only on light scattering (see Chap. 9) or on surface plasmon resonance measurements (see Chap. 13).
Study Protein
Amphipol
CD/
SRCD Fluorescence
RRS/
SERS TRAS Comments
References
8.1
Nicotinic acetylcholine
receptor (nAChR) from
Torpedo marmorata
A8-35
●
Comparative stopped-flow
studies of the binding of a
fluorescent agonist to the
nAChR in native membranes,
in detergent solution, or after
trapping by A8-35
Martinez et al. (2002)
8.2
Rabbit sarcoplasmic Ca
2+
-
ATPase (SERCA1a)
A8-35, SAPol, PMALC12, PMALA-C12
●
Kinetics of dissociation of Ca
2+
from the detergent-solubilized
or APol-trapped ATPase
Picard et al. (2006)
8.3
Bacteriorhodopsin
(BR) from Halobacterium
salinarum
A8-35, NAPols
●
Time-resolved absorbance
spectroscopy (TRAS) studies
of the photocycle of BR either
in its native state (in purple
membrane, detergent, or APols)
or after refolding in either the
presence or absence of lipids,
and either free in solution or
immobilized onto a solid
support
Pocanschi et al. (2006),
Gohon et al. (2008),
Charvolin et al. (2009),
Bazzacco et al. (2012), and
Dahmane et al. (2013)
8.4
OmpA from Escherichia
coli
and FomA from
Fusobacterium nucleatum
A8-35
●
Assessment of refolding
following transfer from urea to
A8-35
Pocanschi et al. (2006, 2013)
8.5
Transmembrane domain
(tOmpA) of E. coli
OmpA
A8-35, FAPol
NBD
●
Förster resonance energy
transfer (FRET) studies of the
exchange of FAPol
NBD for
unlabeled A8-35 or detergent at
the surface of tOmpA
Zoonens et al. (2007) and
Tribet et al. (2009)
8.6
Transmembrane peptides
from subunit a
of the
V-ATPase from
Saccharomyces cerevisiae
A8-35
●
●
CD and intrinsic
fluorescence
studies of the transfer of
transmembrane peptides from
trifluoroethanol to A8-35
Duarte et al. (2008)
8.7
LTB1, LTB2, CB1, and
5-HT
4(a) G protein-coupled
receptors (GPCRs)
A8-35
●
Fluorescence-based titration
assays of ligand binding to
GPCRs folded in A8-35
Dahmane et al. (2009),
Catoire et al. (2010), and
Mary et al. (2014)
(continued)
8.2 Optical Spectroscopy Studies of Amphipols and Membrane Protein/Amphipol Complexes
383