Results 31 to 40 of about 1,294 (176)

Pulling single bacteriorhodopsin out of a membrane: Comparison of simulation and experiment [PDF]

open access: yes, 2006
Mechanical unfolding of single bacteriorhodopsins from a membrane bilayer is studied using molecular dynamics simulations. The initial conformation of the lipid membrane is determined through all-atom simulations and then its coarse-grained ...
Cieplak, Marek   +3 more
core   +1 more source

Wave Mechanics of Ciliary Proteins: Quantum‐Enabled Sensing and Energy Transfer in the “Cellular Antenna”

open access: yesAggregate, Volume 7, Issue 6, June 2026.
This review surveys eukaryotic cilia as putative quantum‐enabled sensory and regulatory centers. It highlights their multifaceted roles in the cell, focuses on the nontrivial roles of quantum mechanics in their membrane and cytoskeletal proteins, and introduces the essential building blocks enabling quantum properties to survive in the warm, wet, and ...
Daniel L. Bilezikian   +5 more
wiley   +1 more source

Photochemical and biochemical modification of bacteriorhodopsin: Optical data storage and hybridbio-materials

open access: yes, 2011
Entwicklung und Evaluierung einer auf Bakteriorhodopsin (BR) basierenden photochromen Tampondruckfarbe. Untersuchungen an neuen langzeitstabilen Photoprodukten von BR und Entwicklung eines biologisch-optischen WORM Datenspeichers und einer ...
Fischer, Thorsten (110793439)
core   +1 more source

FLUORESCENCE STUDIES ON ANTHRYL BACTERIORHODOPSINS

open access: yes, 1991
Fluorescence properties of bacteriorhodopsin analogues containing 3-methyl-5-(9'-anthryl)-2E,4E-pentadienal and 3,7-dimethyl-9-(9'-anthryl)-2E,4E,6E,8E-nonatetraenal chromophores as built-in fluorescence probes are described.
ROY, M   +3 more
core   +1 more source

Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins [PDF]

open access: yes, 1996
According to earlier reports, residue 85 in the bacteriorhodopsin mutants D85E and Y185F deprotonates with two apparent pKa values. Additionally, in Y185F, Asp-85 becomes significantly more protonated during light adaptation. We provide a new explanation
Lanyi, J.K.   +2 more
core   +1 more source

Chromophore equilibria in bacteriorhodopsin

open access: yesBiophysical Journal, 1979
An investigation of the dark equilibria between different chromophores of bacteriorhodopsin (BR) and studies of the kinetics of their interconversion and photochemical activity have led to the following conclusions. (a) A component of the 605-nm chromophore of BR decays in the millisecond range and is likely to be identical to the intermediate O of the
Fischer, U., Oesterhelt, D.
openaire   +2 more sources

Photoisomerization detected in a fully wavelength‐tunable rhodopsin mimic system

open access: yesActa Crystallographica Section D, Volume 82, Issue 6, Page 664-671, June 2026.
The mechanism of retinal photoswitching is illuminated in a designed rhodopsin mimic. Two mechanisms, a conventional cis–trans isomerization and an unprecedented `photodehydration', are observed at atomic resolution in single crystals.We describe the photoisomerization of the retinylidene protonated Schiff base in human retinol‐binding protein II ...
Nona Ehyaei   +10 more
wiley   +1 more source

On the two forms of bacteriorhodopsin

open access: yesFEBS Letters, 1994
In our previous work [(1993) FEBS Lett. 313, 248‐250; (1993) Biochem. Int. 30,461‐469] M‐intermediate formation of wild‐type bacteriorhodopsin was shown to involve two components differing in time constants (τ1 = 60–70 μs and τ2 = 220–250 μs), which were suggested to reflect two independent pathways of M‐intermediate formation.
Komrakov, Andrey Yu., Kaulen, Andrey D.
openaire   +2 more sources

GRKs and arrestins: Nomenclature and functions in GPCR‐dependent and ‐independent signalling

open access: yesBritish Journal of Pharmacology, Volume 183, Issue 11, Page 2619-2633, June 2026.
G protein‐coupled receptor (GPCR) kinases (GRKs) and arrestins play a critical role in the regulation of GPCR signalling. Historic names of mammalian GRKs were replaced by systematic ones in the 1990s; however, both kinds of names are currently in use for mammalian arrestins.
Vsevolod V. Gurevich
wiley   +1 more source

Unravelling the folding of bacteriorhodopsin

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2000
The folding mechanism of integral membrane proteins has eluded detailed study, largely as a result of the inherent difficulties in folding these proteins in vitro. The seven-transmembrane helical protein bacteriorhodopsin has, however, allowed major advances to be made, not just on the folding of this particular protein, but also on the factors ...
openaire   +3 more sources

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