Atom transfer radical polymerization (ATRP), 219
ATRP, see Atom transfer radical polymerization (ATRP)
AUC, see Analytical ultracentrifugation (AUC)
Audebert, R., 153
B
Bacterial flagella, 11
Bacterio-opsin (BO), 334
SRCD spectra before and after APol-assisted
renaturation, 392
uptake of retinal, 289
Bacteriorhodopsin
accessibility of N-terminal tag to solvent in A8-35,
DDM, or NDs, 471
APol-assisted folding, 339–343
APol binding, 274
binding site of retinal, 33
CFE in A8-35, 369
CFE in NAPols, 367, 372, 373
CFE in SAPols, 369
conformational thermostabilization, 84
crystallization by transfer from APols to lipidic
mesophase, 310
crystallization by transfer from NDs to a lipid
mesophase, 118
crystallization from bicelles, 104
DEER study in SMALPs, 421
DMPC-assisted extraction by SMA, 260
EM structure, 35
folding in A8-35, 339–343
folding in NDs, 118
function, 10
functional requirement for a soft environment, 35
function of retinal, 33
immobilization using BAPol, 595, 604
immobilization using OligAPol, 614
integrated into NDs, MD simulation, 113
light- and dark-adapted states, 34
lipid-mediated association of BR trimers into purple
membrane patches, 28
low-resolution 1975 cryo-EM 3D map, 13
MALDI-TOF studies of BR/APol complexes,
633, 634
NAPol-trapped, 167
peptitergent-trapped, 120
photocycle, 33, 34
of BR refolded in A8-35, 341
following complexation by APols, 287
following immobilization using BAPol, 597
proton pumping, 34
rebinding of lipids upon transfer to A8-35, 296
refolding from denatured state, princeps
demonstration, 334
refolding in APG, 164
restoration of protein/lipid interactions after trapping
with A8-35, 287, 296
Schiff base, 32, 33, 289
SEC analysis in SMALPs, 260
sensitivity of the photocycle to lipids, 35
SRCD spectra before and after APol-assisted
renaturation, 392
stability in A8-35 vs. A8-75, 295
stability in APols vs. detergents, 291
stability in OTG vs. purple membrane, 70, 71
stability in sulfonated APols, 295
stabilization by APols, 290–292
structural changes during the photocycle, 35, 36
structure and function (overview), 32–35
as a target for αRep selection using BAPol, 605
as a target for αRep selection using BNAPol, 605
thermal denaturation in APols vs. detergents, 292
3D structure, 34
TM structure, 16
TM topology, 14
trapped in peptide-based NDs, 127
2D NMR spectra in A8-35, DDM and NDs, 472, 473
visible CD spectrum in SMALPs, 392, 393
X-ray structure, 35
Bacteriorhodopsin/A8-35 complexes, 266, 279
analysis by SGSV, 411
concentration by precipitation, 291
consistency and inconsistencies of AUC, SANS, SEC
and EM data, 435
crystallization of BR by transfer to a lipidic
mesophase, 516–522
Eq-AUC analysis, 423, 426
freezing/thawing, 291
lipid composition, 275
lyophilization, 291
model deduced from chemical analysis, AUC
and SANS data, 434, 435
NS EM study of monomeric and aggregated forms,
552–554
radius of gyration, 279
SANS studies, 432, 433
SEC analysis, 417, 418, 447
separation from free A8-35 particles by SGSV
fractionation, 414, 415
SGSV analysis, 413
size relative to BR/DDM complexes, 282
solutions studies, 410
stability in dried films, 396
stabilization by lipids, 292
Stokes radius, 279
surface-enhanced resonance Raman spectroscopy,
396, 397
SV-AUC analysis, 423–425
Bacteriorhodopsin (H. walsbyi)/SMA complexes
crystallization of BR by transfer to a lipidic
mesophase, 521
Bacteriorhodopsin/NAPol complexes, 274
SANS analysis, 436, 437
Bacteriorhodopsin/OligAPol complexes
SEC analysis, 448
Bacteriorhodopsin/SMA complexes
DLS studies, 439
SEC analysis, 439
Baenziger, J.E., 43
690
Index
ATRP, see Atom transfer radical polymerization (ATRP)
AUC, see Analytical ultracentrifugation (AUC)
Audebert, R., 153
B
Bacterial flagella, 11
Bacterio-opsin (BO), 334
SRCD spectra before and after APol-assisted
renaturation, 392
uptake of retinal, 289
Bacteriorhodopsin
accessibility of N-terminal tag to solvent in A8-35,
DDM, or NDs, 471
APol-assisted folding, 339–343
APol binding, 274
binding site of retinal, 33
CFE in A8-35, 369
CFE in NAPols, 367, 372, 373
CFE in SAPols, 369
conformational thermostabilization, 84
crystallization by transfer from APols to lipidic
mesophase, 310
crystallization by transfer from NDs to a lipid
mesophase, 118
crystallization from bicelles, 104
DEER study in SMALPs, 421
DMPC-assisted extraction by SMA, 260
EM structure, 35
folding in A8-35, 339–343
folding in NDs, 118
function, 10
functional requirement for a soft environment, 35
function of retinal, 33
immobilization using BAPol, 595, 604
immobilization using OligAPol, 614
integrated into NDs, MD simulation, 113
light- and dark-adapted states, 34
lipid-mediated association of BR trimers into purple
membrane patches, 28
low-resolution 1975 cryo-EM 3D map, 13
MALDI-TOF studies of BR/APol complexes,
633, 634
NAPol-trapped, 167
peptitergent-trapped, 120
photocycle, 33, 34
of BR refolded in A8-35, 341
following complexation by APols, 287
following immobilization using BAPol, 597
proton pumping, 34
rebinding of lipids upon transfer to A8-35, 296
refolding from denatured state, princeps
demonstration, 334
refolding in APG, 164
restoration of protein/lipid interactions after trapping
with A8-35, 287, 296
Schiff base, 32, 33, 289
SEC analysis in SMALPs, 260
sensitivity of the photocycle to lipids, 35
SRCD spectra before and after APol-assisted
renaturation, 392
stability in A8-35 vs. A8-75, 295
stability in APols vs. detergents, 291
stability in OTG vs. purple membrane, 70, 71
stability in sulfonated APols, 295
stabilization by APols, 290–292
structural changes during the photocycle, 35, 36
structure and function (overview), 32–35
as a target for αRep selection using BAPol, 605
as a target for αRep selection using BNAPol, 605
thermal denaturation in APols vs. detergents, 292
3D structure, 34
TM structure, 16
TM topology, 14
trapped in peptide-based NDs, 127
2D NMR spectra in A8-35, DDM and NDs, 472, 473
visible CD spectrum in SMALPs, 392, 393
X-ray structure, 35
Bacteriorhodopsin/A8-35 complexes, 266, 279
analysis by SGSV, 411
concentration by precipitation, 291
consistency and inconsistencies of AUC, SANS, SEC
and EM data, 435
crystallization of BR by transfer to a lipidic
mesophase, 516–522
Eq-AUC analysis, 423, 426
freezing/thawing, 291
lipid composition, 275
lyophilization, 291
model deduced from chemical analysis, AUC
and SANS data, 434, 435
NS EM study of monomeric and aggregated forms,
552–554
radius of gyration, 279
SANS studies, 432, 433
SEC analysis, 417, 418, 447
separation from free A8-35 particles by SGSV
fractionation, 414, 415
SGSV analysis, 413
size relative to BR/DDM complexes, 282
solutions studies, 410
stability in dried films, 396
stabilization by lipids, 292
Stokes radius, 279
surface-enhanced resonance Raman spectroscopy,
396, 397
SV-AUC analysis, 423–425
Bacteriorhodopsin (H. walsbyi)/SMA complexes
crystallization of BR by transfer to a lipidic
mesophase, 521
Bacteriorhodopsin/NAPol complexes, 274
SANS analysis, 436, 437
Bacteriorhodopsin/OligAPol complexes
SEC analysis, 448
Bacteriorhodopsin/SMA complexes
DLS studies, 439
SEC analysis, 439
Baenziger, J.E., 43
690
Index
