Rhodopsins found in the PURPLE MEMBRANE of halophilic archaea such as HALOBACTERIUM HALOBIUM. Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS.

Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR. (1/1144)

The high-affinity cation-binding sites of bacteriorhodopsin (bR) were examined by solid-state 13C NMR of samples labeled with [3-13C]Ala and [1-13C]Val. We found that the 13C NMR spectra of two kinds of blue membranes, deionized (pH 4) and acid blue at pH 1.2, were very similar and different from that of the native purple membrane. This suggested that when the surface pH is lowered, either by removal of cations or by lowering the bulk pH, substantial change is induced in the secondary structure of the protein. Partial replacement of the bound cations with Na+, Ca2+, or Mn2+ produced additional spectral changes in the 13C NMR spectra. The following conclusions were made. First, there are high-affinity cation-binding sites in both the extracellular and the cytoplasmic regions, presumably near the surface, and one of the preferred cation-binding sites is located at the loop between the helix F and G (F-G loop) near Ala196, consistent with the 3D structure of bR from x-ray diffraction and cryoelectron microscopy. Second, the bound cations undergo rather rapid exchange (with a lifetime shorter than 3 ms) among various types of cation-binding sites. As expected from the location of one of the binding sites, cation binding induced conformational alteration of the F-G interhelical loop.  (+info)

Distortion of the L-->M transition in the photocycle of the bacteriorhodopsin mutant D96N: a time-resolved step-scan FTIR investigation. (2/1144)

The D96N mutant of bacteriorhodopsin has often been taken as a model system to study the M intermediate of the wild type photocycle due to the long life time of the corresponding intermediate of the mutant. Using time-resolved step-scan FTIR spectroscopy in combination with a sample changing wheel we investigated the photocycle of the mutant with microsecond time resolution. Already after several microseconds an intermediate similar to the MN state is observed, which contrasts with the M state of the wild type protein. At reduced hydration M and N intermediates similar to those of wild type BR can be detected. These results have a bearing on the interpretation of the photocycle of this mutant. A mechanism is suggested for the fast rise of MN which provides some insight into the molecular events involved in triggering the opening of the cytosolic channel also of the wild type protein.  (+info)

Molecular modeling of mu opioid receptor and receptor-ligand interaction. (3/1144)

AIM: To construct the 3D structural model of mu opioid receptor (mu OR) and study the interaction between mu OR and fentanyl derivatives. METHODS: The 3D structure of mu OR was modeled using the bacteriorhodopsin (bRh) as a template, in which the alignments of transmembrane (TM) of bRh and mu OR were achieved by scoring the alignment between the amino acid sequence of mu OR and the structure of bRh. The fentanyl derivatives were docked into the 7 helices of mu OR and the binding energies were calculated. RESULTS: (1) The receptor-ligand interaction models were obtained for fentanyl derivatives. (2) In these models, the fundamental binding sites were possibly Asp147 and His297. The negatively charged oxygen of Asp147 and the positively charged ammonium group of ligand formed the potent electrostatic and hydrogen-binding interactions. Whereas the interactions between the positively charged nitrogen of His297 and the carbonyl oxygen of ligand were weak. In addition, there were some pi-pi interactions between the receptor and the ligand. (3) The binding energies of the receptor-ligand complexes had a good correlation with the analgesic activities (-lg ED50) of the fentanyl derivatives. CONCLUSION: This model is helpful for understanding the receptor-ligand interaction and for designing novel mu OR selective ligands.  (+info)

Molecular modeling of interaction between delta opioid receptor and 3-methylfentanylisothiocyanate. (4/1144)

AIM: To construct a 3D structural model of delta opioid receptor (delta OR) and study its interaction with 3-methylfentanylisothiocyanate (SuperFIT). METHODS: Using the bacteriohodopsin as a template, the 3D structure of delta OR was modeled; SuperFIT was docked into its inside. RESULTS: The interaction model between delta OR and (3R, 4S)-SuperFIT was achieved, in which the important binding sites possibly were Asp128, Ser106, Phe104, Tyr308, and Pro315. Asp128 formed the electrostatic and hydrogen-binding interactions with the protonated nitrogen on piperidine of the ligand. Ser106 formed the electrostatic interaction with the N atom of isothiocyano group of the ligand; whereas Phe104, Tyr308, and Pro315 formed the hydrophobic interactions with the S atom of isothiocyano group. In addition, there were some other interactions between delta OR and the ligand. CONCLUSION: The residues Phe104, Tyr308, Pro315, and Ser106 of delta OR are crucial to the delta selectivity of the ligand, which is beneficial for designing novel delta-selective ligand.  (+info)

Interpretation of the spatial charge displacements in bacteriorhodopsin in terms of structural changes during the photocycle. (5/1144)

We have recently introduced a method, made possible by an improved orienting technique using a combination of electric and magnetic fields, that allows the three-dimensional detection of the intramolecular charge displacements during the photocycle of bacteriorhodopsin. This method generates electric asymmetry, a prerequisite for the detection of electric signal on the macroscopic sample, in all three spatial dimensions. Purple membrane fragments containing bacteriorhodopsin were oriented so that their permanent electric dipole moment vectors were perpendicular to the membrane plane and pointed in the same direction. The resulting cylindrical symmetry was broken by photoselection, i. e., by flash excitation with low intensity linearly polarized light. From the measured electric signals, the three-dimensional motion of the electric charge center in the bacteriorhodopsin molecules was calculated for the first 400 microseconds. Simultaneous absorption kinetic recording provided the time-dependent concentrations of the intermediates. Combining the two sets of data, we determined the discrete dipole moments of intermediates up to M. When compared with the results of current molecular dynamics calculations, the data provided a decisive experimental test for selecting the optimal theoretical model for the proton transport and should eventually lead to a full description of the mechanism of the bacteriorhodopsin proton pump.  (+info)

Simulation analysis of the retinal conformational equilibrium in dark-adapted bacteriorhodopsin. (6/1144)

In dark-adapted bacteriorhodopsin (bR) the retinal moiety populates two conformers: all-trans and (13,15)cis. Here we examine factors influencing the thermodynamic equilibrium and conformational transition between the two forms, using molecular mechanics and dynamics calculations. Adiabatic potential energy mapping indicates that whereas the twofold intrinsic torsional potentials of the C13==C14 and C15==N16 double bonds favor a sequential torsional pathway, the protein environment favors a concerted, bicycle-pedal mechanism. Which of these two pathways will actually occur in bR depends on the as yet unknown relative weight of the intrinsic and environmental effects. The free energy difference between the conformers was computed for wild-type and modified bR, using molecular dynamics simulation. In the wild-type protein the free energy of the (13,15)cis retinal form is calculated to be 1.1 kcal/mol lower than the all-trans retinal form, a value within approximately kBT of experiment. In contrast, in isolated retinal the free energy of the all-trans state is calculated to be 2.1 kcal/mol lower than (13,15)cis. The free energy differences are similar to the adiabatic potential energy differences in the various systems examined, consistent with an essentially enthalpic origin. The stabilization of the (13,15)cis form in bR relative to the isolated retinal molecule is found to originate from improved protein-protein interactions. Removing internal water molecules near the Schiff base strongly stabilizes the (13,15)cis form, whereas a double mutation that removes negative charges in the retinal pocket (Asp85 to Ala; Asp212 to Ala) has the opposite effect.  (+info)

Chloride ion binding to bacteriorhodopsin at low pH: an infrared spectroscopic study. (7/1144)

Bacteriorhodopsin (bR) and halorhodopsin (hR) are light-induced ion pumps in the cell membrane of Halobacterium salinarium. Under normal conditions bR is an outward proton transporter, whereas hR is an inward Cl- transporter. There is strong evidence that at very low pH and in the presence of Cl-, bR transports Cl- ions into the cell, similarly to hR. The chloride pumping activity of bR is connected to the so-called acid purple state. To account for the observed effects in bR a tentative complex counterion was suggested for the protonated Schiff base of the retinal chromophore. It would consist of three charged residues: Asp-85, Asp-212, and Arg-82. This quadruplet (including the Schiff base) would also serve as a Cl- binding site at low pH. We used Fourier transform infrared difference spectroscopy to study the structural changes during the transitions between the normal, acid blue, and acid purple states. Asp-85 and Asp-212 were shown to participate in the transitions. During the normal-to-acid blue transition, Asp-85 protonates. When the pH is further lowered in the presence of Cl-, Cl- binds and Asp-212 also protonates. The binding of Cl- and the protonation of Asp-212 occur simultaneously, but take place only when Asp-85 is already protonated. It is suggested that HCl is taken up in undissociated form in exchange for a neutral water molecule.  (+info)

Time-resolved absorption and photothermal measurements with sensory rhodopsin I from Halobacterium salinarum. (8/1144)

An expansion accompanying the formation of the first intermediate in the photocycle of transducer-free sensory rhodopsin I (SRI) was determined by means of time-resolved laser-induced optoacoustic spectroscopy. For the native protein (SRI-WT), the absolute value of the expansion is approximately 5.5 mL and for the mutant SRI-D76N, approximately 1.5 mL per mol of phototransformed species (in 0.5 M NaCl), calculated by using the formation quantum yield for the first intermediate (S610) of Phi610 = 0.4 +/- 0.05 for SRI-WT and 0.5 +/- 0.05 for SRI-D76N, measured by laser-induced optoacoustic spectroscopy and by laser flash photolysis. The similarity in Phi610 and in the determined value of the energy level of S610, E610 = (142 +/- 12) kJ/mol for SRI-WT and SRI-D76N indicates that Asp76 is not directly involved in the first step of the phototransformation. The increase with pH of the magnitude of the structural volume change for the formation of S610 in SRI-WT and in SRI-D76N upon excitation with 580 nm indicates also that amino acids other than Asp76, and other than those related to the Schiff base, are involved in the process. The difference in structural volume changes as well as differences in the activation parameters for the S610 decay should be attributed to differences in the rigidity of the cavity surrounding the chromophore. Except for the decay of the first intermediate, which is faster than in the SRI-transducer complex, the rate constants of the photocycle for transducer-free SRI in detergent suspension are strongly retarded with respect to wild-type membranes (this comparison should be done with great care because the preparation of both samples is very different).  (+info)

Bacteriorhodopsins are a type of protein found in certain archaea, a group of single-celled microorganisms. They are most commonly found in the archaea of the genus Halobacterium, which live in extremely salty environments such as salt lakes and solar salterns.

Bacteriorhodopsins are embedded in the cell membrane of these archaea and contain a retinal molecule, which is a type of vitamin A derivative. When exposed to light, the retinal changes shape, which causes a conformational change in the bacteriorhodopsin protein. This leads to the pumping of protons (hydrogen ions) across the cell membrane, generating a proton gradient.

The proton gradient created by bacteriorhodopsins can be used to generate ATP, which is the main energy currency of the cell. Bacteriorhodopsins are therefore involved in energy production in these archaea and are often referred to as light-driven proton pumps. They have also been studied extensively for their potential applications in optoelectronics and biotechnology.

... (Bop) is a protein used by Archaea, most notably by haloarchaea, a class of the Euryarchaeota. It acts as a ... Bacteriorhodopsin is a light-driven proton pump. It is the retinal molecule that changes its isomerization state from all-trans ... Both rhodopsin and bacteriorhodopsin belong to the 7TM receptor family of proteins, but rhodopsin is a G protein-coupled ... Bacteriorhodopsin has a broad excitation spectrum. For a detection wavelength between 700 and 800 nm, it has an appreciable ...
Lanyi JK (2004). "Bacteriorhodopsin". Annual Review of Physiology. 66: 665-88. doi:10.1146/annurev.physiol.66.032102.150049. ... In the Halobacteria, light-activated ion pumps like bacteriorhodopsin and halorhodopsin generate ion gradients by pumping ions ... "Molecular mechanism of vectorial proton translocation by bacteriorhodopsin". Nature. 406 (6796): 653-57. Bibcode:2000Natur.406 ...
The energy required for the proton pumping reaction may come from light (light energy; bacteriorhodopsins), electron transfer ( ... Bacteriorhodopsin is a light-driven proton pump used by Archaea, most notably in Haloarchaea. Light is absorbed by a retinal ...
"Unfolding pathways of individual bacteriorhodopsins". Science. 288 (5463): 143-6. Bibcode:2000Sci...288..143O. doi:10.1126/ ...
Alignment of bacteriorhodopsins with the yeast sequence YRO2". Pharm. Res. 14 (11): 1533-41. doi:10.1023/a:1012166015402. PMID ...
All-trans-retinal is also an essential component of microbial opsins such as bacteriorhodopsin, channelrhodopsin, and ... Waschuk, Stephen A.; Bezerra, Arandi G.; Shi, Lichi; Brown, Leonid S. (2005). "Leptosphaeria rhodopsin: Bacteriorhodopsin-like ... Ovchinnikov, Yu.A. (8 November 1982). "Rhodopsin and bacteriorhodopsin: structure-function relationships". FEBS Letters. 148 (2 ... "All-trans to 13-cis retinal isomerization in light-adapted bacteriorhodopsin at acidic pH". Journal of Photochemistry and ...
Bacteriorhodopsin, used in some halobacteria as a light-driven proton pump. Hofmann and Lamb use the term opsin in general to ... Ovchinnikov YA (November 1982). "Rhodopsin and bacteriorhodopsin: structure-function relationships". FEBS Letters. 148 (2): 179 ... "Characterization of the primary photochemical events in bacteriorhodopsin and rhodopsin". In Lee AG (ed.). Rhodopsin and G- ...
After the middle of the 1970s, his lab studied the biochemistry of bacteriorhodopsin, a membrane protein that converts light ... Wildenauer, D.; Khorana, H. G. (1977). "The preparation of lipid-depleted bacteriorhodopsin". Biochimica et Biophysica Acta ( ...
Among the many kinds of microbial opsins are the proton pumps bacteriorhodopsin (BR) and xanthorhodopsin (xR), the chloride ... Waschuk SA, Bezerra AG, Shi L, Brown LS (May 2005). "Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a ... doi:10.1016/S1043-9471(05)80049-7. Ovchinnikov, Yu.A. (November 1982). "Rhodopsin and bacteriorhodopsin: structure-function ... and bacteriorhodopsin, are used by various bacterial groups to harvest energy from light to carry out metabolic processes using ...
Prokhorenko, V. I. (2006-09-01). "Coherent Control of Retinal Isomerization in Bacteriorhodopsin". Science. 313 (5791): 1257- ...
After returned to Germany, Oesterhelt showed that physiological function of bacteriorhodopsin is to pump protons out of the ... This protein was isolated and called bacteriorhodopsin. ...
... known today as bacteriorhodopsin. The first bacteriorhodopsin turned out to be of archaeal origin, from Halobacterium salinarum ... Bacteriorhodopsin also lacks the omega loop structure that has been observed at the N-terminus of the structures of several ... Bacteriorhodopsin pumps one Cl− ion, from the extracellular medium into the cytosol, per photon absorbed. Although the ions ... They differ from bacteriorhodopsin in that the claret membrane, in which they are expressed, includes bacterioruberin, a second ...
... by a mechanism similar to that of bacteriorhodopsin. As in bacteriorhodopsin, the retinal chromophore of proteorhodopsin is ... Bacteriorhodopsin was discovered in 1971 and named in 1973 and is currently only known to exist in archaea, not bacteria. ... Bacteriorhodopsin and Halorhodopsin both only exist in archaea whereas proteorhodopsin spans bacteria, archaea, and eukaryotes ... In comparison with its better-known archaeal homolog bacteriorhodopsin, most of the active site residues of known importance to ...
Pyroglutamate is found in many proteins including bacteriorhodopsin. N-terminal glutamic acid and glutamine residues can ...
2. Spin labeling of bacteriorhodopsin mutants at unique cysteines". Biochemistry. 28 (19): 7806-7812. doi:10.1021/bi00445a042. ... Spin Labeling of Bacteriorhodopsin Mutants". Science. 248 (4959): 1088-192. Bibcode:1990Sci...248.1088A. doi:10.1126/science. ...
Large blooms appear reddish, from the pigment bacteriorhodopsin. This pigment is used to absorb light, which provides energy to ...
Large blooms appear reddish, from the pigment bacteriorhodopsin. This pigment is used to absorb light, which provides energy to ...
Waschuk SA, Bezerra AG, Shi L, Brown LS (May 2005). "Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a ...
Another case for this mechanism is Bacteriorhodopsin proton pump. Here the light induced change in the molecular volume is ... "Photoinduced volume changes associated with the early transformations of bacteriorhodopsin: A laser-induced optoacoustic ...
Some examples are bacteriorhodopsin and bacteriophytochromes in some bacteria. See also: phytochrome and phototropism. Most ...
It has also been used in a study of the effects of buffer identity on electric signals of light-excited bacteriorhodopsin. Use ... Tóth-Boconádi R, Dér A, Keszthelyi L (June 2000). "Buffer effects on electric signals of light-excited bacteriorhodopsin". ...
The way bacteriorhodopsin generates a proton gradient in Archaea is through a proton pump. The proton pump relies on proton ... Finally, bacteriorhodopsin returns to its resting state when Asp85 releases its proton to Glu204. PSII also relies on light to ... In bacteriorhodopsin, the proton pump is activated by absorption of photons of 568 nm wavelength which leads to isomerization ... This section will focus on three processes that help establish proton gradients in their respective cells: bacteriorhodopsin ...
He also worked on wave mixing in Bacterio-Rhodopsin, fiber-optics and fiber-optic communications, pulse optics, a new tunable ... "Strong self-defocusing effect and four-wave mixing in bacteriorhodopsin films". Optics Letters. 17 (4): 241-243. Bibcode: ... and phase conjugation with bacteriorhodopsin". Optics Letters. 15 (20): 1117-1119. Bibcode:1990OptL...15.1117W. doi:10.1364/OL. ...
Váró, G.; Eisenstein, L. (1987). "Infrared studies of water induced conformational changes in bacteriorhodopsin". European ... bacteriorhodopsin and rhodopsin. This effort would engage and foster collaborations with scientists including Tom Ebrey, Koiji ...
Some examples are bacteriorhodopsin and bacteriophytochromes in some bacteria. See also: phytochrome and phototropism. Most ... At least some aspects of this response are likely mediated by changes in membrane potential by bacteriorhodopsin, a light- ... "Delta psi-mediated signalling in the bacteriorhodopsin-dependent photoresponse". Journal of Bacteriology. 178 (11): 3008-3014. ...
Herrmann, T. R.; Rayfield, G. W. (1978-02-01). "The electrical response to light of bacteriorhodopsin in planar membranes". ... Simmeth, R.; Rayfield, G. W. (1990-05-01). "Evidence that the photoelectric response of bacteriorhodopsin occurs in less than 5 ... for extensive studies on the optical and electrical properties of bacteriorhodopsin, and ensuing device applications." "George ...
Stuart JA, Brige RR (1996). "Characterization of the primary photochemical events in bacteriorhodopsin and rhodopsin". In Lee ...
Their photosynthetic pigment, bacteriorhodopsin, is actually opaque to the longer-wavelength ultraviolet (its red color). In ... Bacteriorhodopsins isolated from Halobacterium salinarum have been especially studied for their applications in electronics and ... Particularly, bacteriorhodopsins have been used in holographic storage, optical switching, motion detection, and nanotechnology ... Halobacterium can be identified in bodies of water by the light-detecting pigment bacteriorhodopsin, which not only provides ...
"A transposable element from Halobacterium halobium which inactivates the bacteriorhodopsin gene". Proceedings of the National ...
Bacteriorhodopsin - A proton pump used by Haloarchaea to harvest light energy. Boring Billion - a later phase when the seas may ... Many Haloarchaea contain the retinal derivative protein bacteriorhodopsin in their cell membrane, which carries out photon- ...
Bacteriorhodopsin (Bop) is a protein used by Archaea, most notably by haloarchaea, a class of the Euryarchaeota. It acts as a ... Bacteriorhodopsin is a light-driven proton pump. It is the retinal molecule that changes its isomerization state from all-trans ... Both rhodopsin and bacteriorhodopsin belong to the 7TM receptor family of proteins, but rhodopsin is a G protein-coupled ... Bacteriorhodopsin has a broad excitation spectrum. For a detection wavelength between 700 and 800 nm, it has an appreciable ...
The integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal ... Enhanced photocurrent in engineered bacteriorhodopsin monolayer. Patil AV., Premaruban T., Berthoumieu O., Watts A., Davis JJ. ... Amino Acid Substitution, Bacteriorhodopsins, Cysteine, Electrodes, Microscopy, Atomic Force, Mutation, Photons, Solar Energy, ... The integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal ...
Rothschild, K. J., Braiman, M. S., He, Y. W., Marti, T., & Khorana, H. G. (1990). Vibrational spectroscopy of bacteriorhodopsin ... Vibrational spectroscopy of bacteriorhodopsin mutants: Evidence for the interaction of aspartic acid 212 with tyrosine 185 and ... N2 - The role of Asp-212 in the proton pumping mechanism of bacteriorhodopsin (bR) has been studied by a combination of site- ... AB - The role of Asp-212 in the proton pumping mechanism of bacteriorhodopsin (bR) has been studied by a combination of site- ...
Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs journal, June 2006 * Bayburt, Timothy H.; Grinkova, Yelena V ... Functional Cell-free Synthesis of a Seven Helix Membrane Protein: In situ Insertion of Bacteriorhodopsin into Liposomes journal ...
Predicted Bacteriorhodopsin from Exiguobacterium Sibiricum Is a Functional Proton Pump. FEBS Lett. 2010, 584, 4193-4196. [ ... On the other hand, we would like to point out that all the results here are based on the example of bacteriorhodopsin, which is ... we used bacteriorhodopsin from Exiguobacterium sibiricum (ESR) [38,39]. In a sense, rhodopsins are unique objects, since they ... ESR-bacteriorhodopsin from Exiguobacterium sibiricum; LPN-lipid-protein nanodisc; DDM-n-Dodecyl-β-D-Maltoside; DHPC-DH6PC, 1,2- ...
INTRODUCTION Bacteriorhodopsin (bR) is a purple membrane protein that acts as a light-driven proton pump in (Oesterhelt and ... For wild-type bacteriorhodopsin, the global conformational CLG4B modification is linked to the structural rearrangement of ... The light-driven proton pump bacteriorhodopsin (bR) is a transmembrane protein that. The light-driven proton pump ... The vectorial proton migration through the bacteriorhodopsin pump can be closely from the set of regional and global ...
Publications] Kataoka, Mikio: Time-resolved X-ray Diffraction Studies on Purple Membrane and Bacteriorhodopsin (II). PF ... Publications] Iwasa, Tatsuo: Photochemical reactions of bacteriorhodopsin in Triton X-100 solution studied by low temperature ... Publications] Tokunaga, Fumio: X-ray Diffraction of Bacteriorhodopsin with Nitrated Tyrosine Residues. PF Activity Report. 3 ... Publications] Tokunaga, Fumio: X-ray Diffraction of Bacteriorhodopsin with Nitrated Tyrosine Residues (II). PF Activity ...
2002) Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the re-protonation ... 2002) High-throughput screening of bacteriorhodopsin mutants in whole cell pastes. Biochimica et Biophysica Acta (BBA) - ...
Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science 361:eaat0094 ... Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science 361:eaat0094 ...
Characterization of proline-containing alpha-helix (helix F model of bacteriorhodopsin) by molecular dynamics studies. Proteins ...
Jan, Lily Kung-Chung Yeh (1974) Investigations on rhodopsin and bacteriorhodopsin. I. Ultrastructural localization of rhodopsin ... The isomeric configuration of the bacteriorhodopsin chromophore. Dissertation (Ph.D.), California Institute of Technology. doi: ...
I am trying to simulate bacteriorhodopsin in a lipid membrane but in , charmm , , topology there is not topology for retinal. I ...
Presentation] Reconstitution of bacteriorhodopsin into partially fluorinated phosphatidylcholine liposomes2011. *. Author(s). ... Presentation] Decay kinetics of the M photointermediate of bacteriorhodopsin in short chain phosphatidylcholine micelles2011. * ...
... of the resonance Raman spectra in the fingerprint region for the initial picosecond interval of the bacteriorhodopsin ...
Kietis, B. P., Saudargas, P., Varo, G., Valkunas, L., External electric control of the proton pumping in bacteriorhodopsin, Eur ... Mechanism of proton transfer in bacteriorhodopsin * Structure-based model of fucoxanthin-chlorophyll protein complex: ... External electric control of the proton pumping in bacteriorhodopsin. 2007-01-01 00:00 ...
Part I. Bacteriorhodopsin-related materials work for molecular electronics. Part II. Volumetric optical memory based on the ... branched photocycle of bacteriorhodopsin. Part III. The role of calcium in the bacteriorhodopsin binding site, Jeffrey Alan ...
The research was mainly focused on the expression of bacteriorhodopsin and its functional properties. In contrast, less is ... The research was mainly focused on the expression of bacteriorhodopsin and its functional properties. In contrast, less is ...
Description: English: Cutaway view of bacteriorhodopsin from Halobacterium salinarum, with the retinol cofactor and residues ...
Bacteriorhodopsin Registry Number. 53026-44-1. CAS Type 1 Name. Bacteriorhodopsins. Previous Indexing. Bacterial Proteins (1974 ... Bacteriorhodopsins Preferred Term Term UI T431730. Date12/26/2000. LexicalTag NON. ThesaurusID NLM (2002). ... Bacteriorhodopsins Preferred Concept UI. M0002142. Registry Number. 53026-44-1. Scope Note. Rhodopsins found in the PURPLE ... Bacteriorhodopsin Term UI T004193. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ...
Bacteriorhodopsin use Bacteriorhodopsins Bacteriorhodopsins Bacteriostat use Thiram Bacterium Host Interactions use Host ...
Bacteriorhodopsin use Bacteriorhodopsins Bacteriorhodopsins Bacteriostat use Thiram Bacteriuria Bacteriurias use Bacteriuria ...
BACTERIORHODOPSIN. BACTERIORHODOPSINS. DOPA. DIHYDROXYPHENYLALANINE. GABA. GAMMA-AMINOBUTYRIC ACID. XANTHOPHYLL. LUTEIN. D03 - ...
4. Bacteriorhodopsin: Exclusive to halobacteria, bacteriorhodopsin is a pigment that consists of a protein linked to a retinal ...
23. BACTERIORHODOPSIN [ԲԱԿՏԵՐԻՈՐՈԴՈՊՍԻՆ] ◊ [ԲԱԿՏԵՐԻՈՐՈԴՈՊՍԻՆ] 73. BASKETBALL [ԲԱՍԿԵՏԲՈԼ] 24. BACTERIURIA [ԲԱԿՏԵՐԻԱՄԶՈՒԹՅՈՒՆ ...
4. cells containing bacteriorhodopsin. 5. the presence of very large numbers of ion pumps in its plasma membrane. A) 2 and 5. B ...
Knowledge-based design of a soluble bacteriorhodopsin. Protein engineering 10 (10), 1175-1190, October 1, 1997.. CJ Gibas, S ...
"Terahertz Spectroscopy Of Bacteriorhodopsin And Rhodopsin: Similarities And Differences". Biophysical Journal 94 (2008): 3217- ... "Terahertz Measurements Of The Photoactive Protein Bacteriorhodopsin Mutant D96N: M And P States". Mater. Res. Soc. Symp. ... "Terahertz Time Domain Spectroscopy Of The M Intermediate State Of Bacteriorhodopsin". Proceedings Of The 26Th International ... A Comparison Of Collective Vibrational Modes Of Wild-Type And D96N Bacteriorhodopsin". Biophysical Journal 85 (2003): 1269-1277 ...
These spots have that there is even a basic bacteriorhodopsin, if any, between representation on the one diversity and ... The download southeast asian muslims in the era of globalization in NLF in virtue bacteriorhodopsin lawn( IMISX) use accepted ... How is this for a uncertainty bacteriorhodopsin appropriate time? Microsoft Surface Book 2: Electric Boogaloo. Where obtained ... mass campaigns like Medicare and Medicaid do actually 69 bacteriorhodopsin of images; consumers, 19 cause; and Acoustic resin, ...
  • Bacteriorhodopsin is a light-driven proton pump. (wikipedia.org)
  • The light-driven proton pump bacteriorhodopsin (bR) is a transmembrane protein that uses large conformational changes for proton transfer from the cytoplasmic to the extracellular regions. (researchensemble.com)
  • INTRODUCTION Bacteriorhodopsin (bR) is a purple membrane protein that acts as a light-driven proton pump in (Oesterhelt and Stoeckenius, 1971). (researchensemble.com)
  • Bacteriorhodopsin (bR) is a transmembrane protein that functions as a light-driven proton pump in halophilic archaea. (bvsalud.org)
  • The proton-conducting pathway of bacteriorhodopsin (BR) contains at University, PO Box 124 least nine internal water molecules that are thought to be key players in SE-22100 Lund, Sweden the proton translocation mechanism. (lu.se)
  • Bacteriorhodopsin (BR), the light-driven proton two half-channels. (lu.se)
  • The role of Asp-212 in the proton pumping mechanism of bacteriorhodopsin (bR) has been studied by a combination of site-directed mutagenesis and Fourier transform infrared difference spectroscopy. (syr.edu)
  • The vectorial proton migration through the bacteriorhodopsin pump can be closely from the set of regional and global conformational adjustments in the K, L, M1, M2, N, and O TMC-207 novel inhibtior intermediates. (researchensemble.com)
  • Description: English: Cutaway view of bacteriorhodopsin from Halobacterium salinarum, with the retinol cofactor and residues involved in proton transfer (Arg82, Asp85, Asp96) shown as ball and stick models. (eol.org)
  • Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS . (nih.gov)
  • They are critical in understanding the function of various proton pumps such as bacteriorhodopsin (BR) and cytochrome oxidase C. Their light or redox driven action and unidirectional proton pumping mechanism motivates the structural study of these membrane proteins. (lu.se)
  • The integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal of interest for some two decades or more and holds significant promise from the perspective of derived photoresponse or energy capture interfaces. (ox.ac.uk)
  • For wild-type bacteriorhodopsin, the global conformational CLG4B modification is linked to the structural rearrangement of cytoplasmic helices and loops from the first intermediates (K, L, and M1) to the later on intermediates (M2, N, and O) (Subramaniam et al. (researchensemble.com)
  • 2002) Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the re-protonation mechanism. (covenant.edu)
  • 2002) High-throughput screening of bacteriorhodopsin mutants in whole cell pastes. (covenant.edu)
  • Bacteriorhodopsin (Bop) is a protein used by Archaea, most notably by haloarchaea, a class of the Euryarchaeota. (wikipedia.org)
  • By expressing bacteriorhodopsin, the archaea cells are able to synthesise ATP in the absence of a carbon source. (wikipedia.org)
  • analysis targets how the environment adjusts to these two states and on how the dynamics of the helices, loops, and water molecules can be related to the pump mechanism of bacteriorhodopsin. (researchensemble.com)
  • Bacteriorhodopsin is a 27 kDa integral membrane protein usually found in two-dimensional crystalline patches known as "purple membrane", which can occupy almost 50% of the surface area of the archaeal cell. (wikipedia.org)
  • The movie created from the measurements at SLS shows how the structure of the bacteriorhodopsin molecule changes in the next 200 milliseconds after it is activated by light. (sciencemission.com)
  • The membrane protein bacteriorhodopsin (BR) can be kept soluble in its native state for months in the absence of detergent by amphipol (APol) A8-35, an amphiphilic polymer. (nih.gov)
  • INTRODUCTION Bacteriorhodopsin (bR) is a purple membrane protein that acts as a light-driven proton pump in (Oesterhelt and Stoeckenius, 1971). (researchensemble.com)
  • The protein bacteriorhodopsin occurs in microorganisms that live on the surface of lakes, streams, and other bodies of water. (sciencemission.com)
  • The light-driven proton pump bacteriorhodopsin (bR) is a transmembrane protein that uses large conformational changes for proton transfer from the cytoplasmic to the extracellular regions. (researchensemble.com)
  • LambdaVision constructs the artificial retina using alternating layers of a light-sensitive protein called bacteriorhodopsin and a polymer on a scaffold material commonly used in medical devices. (loriacarrinc.com)
  • To understand the specific, atomic-level, details of the electrogenic transport of protons across the membrane, our NHLBI collaborator uses spectrophotometry to study the rapid kinetics of the simple, photon-driven, proton pump bacteriorhodopsin (BR). (nih.gov)
  • Primary attention has been on integral membrane, energy-transducing, proton pumps, namely cytochrome oxidase and bacteriorhodopsin (BR). (nih.gov)
  • Bacteriorhodopsins function as an energy transducers, converting light energy into electrochemical energy via PROTON PUMPS . (nih.gov)
  • analysis targets how the environment adjusts to these two states and on how the dynamics of the helices, loops, and water molecules can be related to the pump mechanism of bacteriorhodopsin. (researchensemble.com)
  • Single molecule kinetics of bacteriorhodopsin by HS-AFM. (cornell.edu)
  • The absorbance changes that accompany the light-driven proton-pumping cycle of bacteriorhodopsin measured over a broad range of times, wavelengths, temperatures, and pH values have been globally fitted to the kinetic model K in equilibrium with L in equilibrium with X in equilibrium with M in equilibrium with N in equilibrium with O----bR. (nih.gov)
  • The equilibrium side chain orientations of tryptophan and tyrosine residues are discussed and compared with those found in the recently proposed model of bacteriorhodopsin. (nih.gov)
  • With the new method at SLS, we can now follow the last part of the movement of bacteriorhodopsin, where the steps are in the millisecond range', explains first author of the paper. (sciencemission.com)
  • Pulling single bacteriorhodopsin out of a membrane: Comparison of simulation and experiment. (bioexploratorium.pl)
  • For wild-type bacteriorhodopsin, the global conformational CLG4B modification is linked to the structural rearrangement of cytoplasmic helices and loops from the first intermediates (K, L, and M1) to the later on intermediates (M2, N, and O) (Subramaniam et al. (researchensemble.com)
  • In the present case, molecular dynamics (MD) studies are carried out on helix F model of bacteriorhodopsin (BR) Ace-(Ala)7-Trp-(Ala)2-Tyr-Pro-(Ala)2-Trp- (Ala)8-NHMe and compared with Ace-(Ala)7-Trp-(Ala)2-Tyr-(Ala)3-Trp-(Ala)8-NHMe in which the proline is replaced by alanine. (nih.gov)