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1 ter-characterized membrane protein (Asp85 in bacteriorhodopsin).
2 on gradients or the light-driven proton pump bacteriorhodopsin.
3 hanges to those caused by dark adaptation in bacteriorhodopsin.
4 ntly, does not denature the membrane protein bacteriorhodopsin.
5 24-O(gamma) hydrogen bond does not stabilize bacteriorhodopsin.
6 on transport cycle of the light-driven pump, bacteriorhodopsin.
7 ules can be related to the pump mechanism of bacteriorhodopsin.
8 observed for the light-activated proton pump bacteriorhodopsin.
9 nts of the light-driven proton/hydroxyl-pump bacteriorhodopsin.
10 s a biological detergent that can solubilize bacteriorhodopsin.
11 lent binding of retinal and final folding to bacteriorhodopsin.
12 ated at the extracellular side in helix C of bacteriorhodopsin.
13 lles, containing retinal, to give functional bacteriorhodopsin.
14 part of the proton release complex (PRC) in bacteriorhodopsin.
15 torial, light-driven transport of protons by bacteriorhodopsin.
16 (a) of the retinal protonated Schiff base in bacteriorhodopsin.
17 s has been quantified for frozen crystals of bacteriorhodopsin.
18 luation of the last proton transfer steps in bacteriorhodopsin.
19 tion making it comparable to the proton pump bacteriorhodopsin.
20 sporter distantly related to the proton pump bacteriorhodopsin.
21 roton transport cycle of the related protein bacteriorhodopsin.
22 ually stable, single domain proteins such as bacteriorhodopsin.
23 hromophore within the membrane-bound protein bacteriorhodopsin.
24 intermediate in the ion-motive photocycle of bacteriorhodopsin.
25 rate and yield of another membrane protein, bacteriorhodopsin.
26 re, we directly determine the flexibility of bacteriorhodopsin -- a protein that uses the energy in l
27 capabilities of proteins and, in the case of bacteriorhodopsin, a 700-fold improvement has been reali
28 ur experiments demonstrate that in wild-type bacteriorhodopsin, a large protein conformational change
30 in situ isomerization dynamics of retinal in bacteriorhodopsin, a microbial retinal protein that func
34 the Halobacterium sp. NRC-1 genome, reduced bacteriorhodopsin accumulation on solid medium but not i
36 lutamate residue corresponding to Asp(85) in bacteriorhodopsin acts as the primary acceptor of the Sc
37 eubacterial MP, (ii) Halobacterium salinarum bacteriorhodopsin, an alpha-helical archaebacterial MP w
42 of heptahelical membrane proteins related to bacteriorhodopsin and characterized by a duplicated moti
43 ptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular
44 ared, for the Glu-194 and Glu-204 mutants of bacteriorhodopsin and detected an anomalous O state, lab
45 stitutions at 24 positions in the B helix of bacteriorhodopsin and examined their effects on structur
46 of helical membrane proteins, we found that bacteriorhodopsin and halorhodopsin are the most tightly
47 -200-Thr and Val-210-Tyr), expected to align bacteriorhodopsin and HtrII in similar juxtaposition as
48 on of the structured EF interhelical loop of bacteriorhodopsin and its change in the M photointermedi
49 ever, deletion of both brp and blh abolished bacteriorhodopsin and retinal production in liquid mediu
50 is supported by experiments carried out with bacteriorhodopsin and rhodopsin, in which cutting or eli
51 photoproduct(s) M' were studied in wild-type bacteriorhodopsin and several mutants at low temperature
52 of reactions in the photocycles of wild-type bacteriorhodopsin and several site-specific mutants.
53 relation between the binding of one Ca2+ per bacteriorhodopsin and the amount of blue membrane conver
54 ed at individual sites throughout helix D of bacteriorhodopsin and the changes in the fluorescence of
55 he visible absorbance maxima of ground state bacteriorhodopsin and the mean decay times of the photoc
57 pairwise helix-helix interaction surfaces of bacteriorhodopsin and three other seven-transmembrane-he
58 imine similar to the pKa changes observed in bacteriorhodopsin and visual opsins during isomerization
59 ApoA lipoprotein enhanced the solubility of bacteriorhodopsin and would facilitate functional studie
60 idues (the homologs of Asp-85 and Asp-212 in bacteriorhodopsin) and an arginine residue (the homolog
61 ransmembrane G protein-coupled receptor-like bacteriorhodopsin, and cytochrome P450s (peripheral MPs)
62 orylation in mitochondria, proton pumping in bacteriorhodopsin, and uncoupling membrane potentials by
63 absorption spectrum, opposite of the case of bacteriorhodopsin; and (iii) efficient reversible light-
64 tually all successful photonic devices using bacteriorhodopsin are based on chemical or genetic varia
65 or groups, corresponding to D212 and D115 in bacteriorhodopsin, are clearly different from other micr
66 structural changes of the membrane protein, bacteriorhodopsin, are studied during the premelting rev
67 , the homologues of the Asp-85 and Asp-96 in bacteriorhodopsin, are the proton acceptor and donor to
68 niques for the extramembranous domains using bacteriorhodopsin as a scaffold for membrane attachment
69 esponds well with estimates for mutations in bacteriorhodopsin as well as for those mutations in the
70 o photoactive protein systems, rhodopsin and bacteriorhodopsin, as a means to characterize collective
71 ral information is available for the initial bacteriorhodopsin, as well as the first five states in t
72 oxylic acids of the light-driven proton pump bacteriorhodopsin, Asp-85 and Asp-96, were replaced, sho
73 These include Asp73, which in the case of bacteriorhodopsin (Asp85) functions as the Schiff base c
75 ) studies of the photocycle intermediates of bacteriorhodopsin at cryogenic temperatures, water molec
79 e was constructed and docked into a helical, bacteriorhodopsin-based model of the recently identified
80 the current fabrication technique, versatile bacteriorhodopsin-based photoelectric immunosensors can
81 d regulation of carotenoid metabolism during bacteriorhodopsin biogenesis, we have identified an H. s
84 rometer as a passive structure, covered by a bacteriorhodopsin (bR) adlayer as the active element.
85 n orientation to two transmembrane proteins, bacteriorhodopsin (bR) and F(0)F(1)-ATP synthase; the so
86 Previous work with the alpha-helical MPs bacteriorhodopsin (bR) and glycophorin A (GpA) shows tha
92 surfactants to the integral membrane protein bacteriorhodopsin (BR) and the formation of protein-surf
94 ion on the protein conformational changes of bacteriorhodopsin (bR) as a function of temperature.
95 mperature dependence of the FT-IR spectra of bacteriorhodopsin (bR) as a function of the pH and of th
97 of cryo-trapped photocycle intermediates of bacteriorhodopsin (bR) by a factor of approximately 90.
99 were conducted on purple membrane containing bacteriorhodopsin (bR) deposited on gold, aluminum/alumi
105 ole of proline residues in the photocycle of bacteriorhodopsin (bR) is addressed using solid-state NM
107 d below 2000 cm(-1) upon exciting retinal in bacteriorhodopsin (bR) is found to have a rise time in t
109 of the steps in the proton pumping cycle of bacteriorhodopsin (BR) is the release of a proton from t
110 thod for quantifying the dissociation of the bacteriorhodopsin (BR) lattice, a naturally occurring tw
112 olecular transformations in a self-assembled bacteriorhodopsin (bR) monolayer are monitored by observ
114 e purple membrane (PM) lattice, the earliest bacteriorhodopsin (BR) photocycle intermediates, and div
117 d with proton translocation steps during the bacteriorhodopsin (BR) photocycle were determined by tim
120 made by fusing proteoliposomes containing a bacteriorhodopsin (bR) proton pump onto the nanowire sur
121 nvestigated the role of the native lipids on bacteriorhodopsin (bR) proton transfer and their connect
122 FX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 A resolution and a method
123 r the bR(555), bR(568), and M(412) states of bacteriorhodopsin (bR) using solid-state NMR spectroscop
126 o be important for the proper functioning of bacteriorhodopsin (BR), a light-driven proton pump.
129 The high stability of the membrane protein bacteriorhodopsin (bR), an archetypal member of the rhod
130 metry (MS) method allows for the analysis of bacteriorhodopsin (BR), an integral membrane protein tha
131 g been recognized as an important residue in bacteriorhodopsin (bR), because its mutation usually res
132 al rhodopsins, in particular the proton pump bacteriorhodopsin (BR), than to earlier known channelrho
134 osition dependence of photocycle kinetics of bacteriorhodopsin (bR), transient absorption spectroscop
135 culations on the 1.55 A crystal structure of bacteriorhodopsin (bR), we identify the principal molecu
136 set obtained through mechanical unfolding of bacteriorhodopsin (bR), which contained a significant nu
145 f a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light e
146 ssess the rate of folding from SDS-denatured bacteriorhodopsin (bRU) and provides accurate thermodyna
150 he Arg-82 homolog that fulfills this role in bacteriorhodopsin caused minimal spectral changes in the
151 Adding Ca2+ or other cations to deionized bacteriorhodopsin causes a blue to purple color shift, a
153 with a rate constant of 0.00033 s-1 to give bacteriorhodopsin containing all trans and 13 cis-retina
156 ch is demonstrated using cell-free expressed bacteriorhodopsin coupled to a quartz glass surface in a
157 ed the L intermediate of the photocycle in a bacteriorhodopsin crystal in photo-stationary state at 1
159 l generated from molecular modeling based on bacteriorhodopsin crystallographic structure indicated t
163 e microscopy the morphology of in cubo grown bacteriorhodopsin crystals in inert buffers and during e
164 rared absorption bands, recorded from single bacteriorhodopsin crystals, confirm that the M-substate
166 effect of divalent ion binding to deionized bacteriorhodopsin (dI-bR) on the thermal transitions of
167 n of the secondary and tertiary structure of bacteriorhodopsin during its in vitro refolding from an
169 the photoactive sites of proteorhodopsin and bacteriorhodopsin during the primary photoreaction.
171 investigated whether the known structure of bacteriorhodopsin exhibited any similarity in its active
172 involved OFETs integrating phospholipids and bacteriorhodopsin exposed to 1-5% anesthetic doses that
173 e primary photochemical event in an oriented bacteriorhodopsin film is measured by directly probing t
174 y directly probing the electric field in the bacteriorhodopsin film using an ultrafast electro-optic
175 ctions after illumination of 100% humidified bacteriorhodopsin films was followed with FTIR spectrosc
178 shapes and optimize retinal isomerization in bacteriorhodopsin, for excitation levels up to 1.8 x 10(
186 n recent years, structural information about bacteriorhodopsin has grown substantially with the publi
187 er with previous work, this study shows that bacteriorhodopsin has to populate at least two folding i
188 the ionizable groups in the resting state of bacteriorhodopsin have been carried out using the recent
190 three membrane-embedded proline residues of bacteriorhodopsin have been replaced individually by ala
191 onnecting the seven transmembrane helices of bacteriorhodopsin have each been replaced in turn by str
193 e spectral tuning difference with respect to bacteriorhodopsin: (i) repositioning of the guanidinium
194 unds of the storage of the release proton in bacteriorhodopsin in a hydrogen-bonded water network.
196 lar to those previously reported for folding bacteriorhodopsin in detergent or lipid micelles, except
199 Biogenesis of the light-driven proton pump bacteriorhodopsin in the archaeon Halobacterium salinaru
200 vealed unexpected differences between NR and bacteriorhodopsin in the configuration of the retinal ch
201 c parts of the heptahelical membrane protein bacteriorhodopsin in the mutant R82A and its second site
203 holipids (TRITC-DHPE) and membrane proteins (bacteriorhodopsin) in a planar polymer-tethered 1-stearo
204 polar residue, tyrosine 199, not present in bacteriorhodopsin, in the middle of the membrane bilayer
205 ions of the tryptophan residues in wild-type bacteriorhodopsin, in the resting state, and in critical
206 for the last photocycle intermediate (O) of bacteriorhodopsin, in which Asp85 is protonated, the pro
207 re, time-resolved FTIR difference spectra of bacteriorhodopsin, including the water O-H stretching vi
208 ding step in the SDS-induced denaturation of bacteriorhodopsin involves a reduction in alpha-helical
209 ures provide insight into how this mutant of bacteriorhodopsin is able to bind a variety of different
210 he chromophore binding site of light-adapted bacteriorhodopsin is analyzed by using modified neglect
212 inal Schiff base in chymotryptically cleaved bacteriorhodopsin is reduced to a secondary retinylamine
213 polyene chain of the retinal chromophore in bacteriorhodopsin is studied using molecular dynamics si
214 key event in light-driven proton pumping by bacteriorhodopsin is the formation of the L intermediate
215 elates with the fact that the FG loop mutant bacteriorhodopsin is the most susceptible to denaturatio
217 ermediate in the proton-motive photocycle of bacteriorhodopsin is the starting state for the first pr
218 inding cavity such as those of rhodopsin and bacteriorhodopsin, is also a dominant reaction pathway f
219 s the transducer, which contains photoactive bacteriorhodopsin, is here first demonstrated for direct
220 ion of the retinal protonated Schiff-base in bacteriorhodopsin, isorhodopsin and rhodopsin, all of wh
221 structure of the homologous retinal protein, bacteriorhodopsin, it is not clear where the carotenoid
224 nergy (0.20-0.41 eV) is required for optimal bacteriorhodopsin liberation on the FT-ICR, in compariso
225 plasmic and extracellular surface domains of bacteriorhodopsin mediated by salt bridges and hydrogen-
226 The photovoltaic behavior of films in which bacteriorhodopsin molecules are embedded in a polyvinyl
227 n, we reexamined the unfolding of individual bacteriorhodopsin molecules in native lipid bilayers.
229 action structure of the non-illuminated D96A bacteriorhodopsin mutant reveals structural changes as f
230 ons, the seven-transmembrane helical protein bacteriorhodopsin-octylglucoside micelle and the empty n
231 protein of marine proteobacteria similar to bacteriorhodopsin of the archaea, is a light-driven prot
232 we simulated two conformations of wild-type bacteriorhodopsin, one of the dark-adapted state and the
233 it does not perturb either the structure of bacteriorhodopsin or the nature of the light-activated c
235 of an early M-intermediate of the wild-type bacteriorhodopsin photocycle formed by actinic illuminat
236 tion of the pigment and the last step of the bacteriorhodopsin photocycle imply low barriers against
239 The K state, an early intermediate of the bacteriorhodopsin photocycle, contains the excess free e
240 by structures of intermediate states in the bacteriorhodopsin photocycle, this study also suggests t
245 nto the heterotrophic, oxygen-respiring, and bacteriorhodopsin-photosynthetic haloarchaeal common anc
246 es, and the lipid-induced recovery of native bacteriorhodopsin properties in terms of the visible abs
250 rganized transmembrane protein arrays: (i) a bacteriorhodopsin purple membrane-like structure where p
253 gineered human beta2-adrenergic receptor and bacteriorhodopsin revealed a number of factors that incr
254 olved resonance Raman vibrational spectra of bacteriorhodopsin's key J and K photoisomerization inter
256 wledge, that transmembrane proteins, such as bacteriorhodopsin, sarcoplasmic reticulum Ca(2+)ATPase (
257 those of other microbial rhodopsins such as bacteriorhodopsin, sensory rhodopsin II, and Neurospora
258 ve-site residue corresponding to Asp(212) in bacteriorhodopsin serves as an alternative proton accept
259 were both able to keep the membrane protein bacteriorhodopsin stable, one of them for at least 3 mon
260 rane of Halobacteria are required for normal bacteriorhodopsin structure, function, and photocycle ki
261 sequent retinal binding and final folding to bacteriorhodopsin, suggesting that these proline residue
262 ubstantial differences relative to wild-type bacteriorhodopsin, suggesting that they represent inhere
264 ex of bacterioopsin (Bop) and retinal called bacteriorhodopsin that functions as a light-driven proto
265 The folding of the transmembrane protein bacteriorhodopsin that occurs during the binding of its
266 al-binding integral membrane proteins called bacteriorhodopsins that function as light-driven proton
267 as the dynamic phase transition, although in bacteriorhodopsin the latter is usually believed to take
269 and tested on the integral membrane protein, bacteriorhodopsin, the crystal structure of which had pr
271 zation in the initial photochemical event in bacteriorhodopsin, the primary photoproduct K makes a th
272 ing the high-resolution crystal structure of bacteriorhodopsin, there are no obvious helix-helix inte
273 asurements of wild-type (WT) and D96N mutant bacteriorhodopsin thin films have been carried out using
274 by the corresponding residues in SRII enable bacteriorhodopsin to efficiently relay the retinal photo
275 observe, however, that the three prolines in bacteriorhodopsin transmembrane helices can be changed t
277 vailable for all of the intermediates of the bacteriorhodopsin transport cycle, and they describe the
278 ere calculated in nine crystal structures of bacteriorhodopsin trapped in bR, early M, and late M sta
279 s applied to the photoactivated proton pump, bacteriorhodopsin, using conformational free energy diff
281 a light-triggered electrochemical gradient, bacteriorhodopsin was co-reconstituted with the permease
282 fect on the overall structure of a Nanodisc, bacteriorhodopsin was embedded into a Nanodisc and simul
285 A spin-label at site 101 in the C-D loop of bacteriorhodopsin was previously found to detect a confo
286 1, originating from the initial unphotolyzed bacteriorhodopsin, was observed as a trough in the diffe
287 13 peptides, spanning the entire sequence of bacteriorhodopsin, was synthesized, and the structures o
288 nidirectional transmembrane ion transport in bacteriorhodopsin, we determined the atomic structures o
289 nformations in the structure and function of bacteriorhodopsin, we have constructed bacterioopsin gen
291 hyl bonds of the retinylidene chromophore of bacteriorhodopsin were investigated in the M photointerm
292 C), a complex in the extracellular domain of bacteriorhodopsin where an excess proton is shared by a
293 zed a unique divalent cation binding site on bacteriorhodopsin which controls the blue-to-purple tran
294 oped striking light-powered proteins such as bacteriorhodopsin, which can convert light energy into c
295 ose-binding protein and the membrane protein bacteriorhodopsin, which display moderate to weak coupli
296 is in the space occupied by a tryptophan in bacteriorhodopsin, which is replaced by the smaller glyc
299 tained reliable phi-values for 16 mutants of bacteriorhodopsin with good coverage across the protein.
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