نتایج جستجو برای: bacteriorhodopsin br

تعداد نتایج: 41878  

Journal: :Biophysical journal 2012
Patrick D Bosshart Patrick L T M Frederix Andreas Engel

Single-molecule force spectroscopy has become a versatile tool for investigating the (un)folding of proteins and other polymeric molecules. Like other single-molecule techniques, single-molecule force spectroscopy requires recording and analysis of large data sets to extract statistically meaningful conclusions. Here, we present a data analysis tool that provides efficient filtering of heteroge...

2015
Hila Einati Debabrata Mishra Noga Friedman Mordechai Sheves Ron Naaman

The role of the electron spin in chemistry and biology has received much attention recently owing to to the possible electromagnetic field effects on living organisms and the prospect of using molecules in the emerging field of spintronics. Recently the chiral-induced spin selectivity effect was observed by electron transmission through organic molecules. In the present study, we demonstrated t...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Erik Freier Steffen Wolf Klaus Gerwert

High-resolution protein ground-state structures of proton pumps and channels have revealed internal protein-bound water molecules. Their possible active involvement in protein function has recently come into focus. An illustration of the formation of a protonated protein-bound water cluster that is actively involved in proton transfer was described for the membrane protein bacteriorhodopsin (bR...

Journal: :Biochemistry 2008
Richard W Hendler Richard I Shrager Curtis W Meuse

In 1995, evidence both for photocooperativity and for heterogeneity as possible explanations for the ability of actinic light to modify the kinetics and pathways of the bacteriorhodopsin (BR) photocycle was reviewed ( Shrager, R. I., Hendler, R. W., and Bose, S. (1995) Eur. J. Biochem. 229, 589-595 ). Because both concepts could be successfully modeled to experimental data and there was suggest...

Journal: :Biophysical journal 1997
W Humphrey E Bamberg K Schulten

Molecular dynamics simulations of wild-type bacteriorhodopsin (bR) and of its D85N, D85T, D212N, and Y57F mutants have been carried out to investigate possible differences in the photoproducts of these proteins. For each mutant, a series of 50 molecular dynamics simulations of the photoisomerization and subsequent relaxation process were completed. The photoproducts can be classified into four ...

2010
Sukhdev Roy Mohit Prasad Juraj Topolancik Frank Vollmer

We show all-optical switching of an input infrared laser beam at 1310 nm by controlling the photoinduced retinal isomerization to tune the resonances in a silica microsphere coated with three bacteriorhodopsin BR protein monolayers. The all-optical tunable resonant coupler re-routes the infrared beam between two tapered fibers in 50 s using a low power 200 W green 532 nm and blue 405 nm pump be...

Journal: :The EMBO journal 1989
A Blanck D Oesterhelt E Ferrando E S Schegk F Lottspeich

The gene coding for sensory rhodopsin I (SR-I) has been identified in a restriction fragment of genomic DNA from the Halobacterium halobium strain L33. Of the 1014 nucleotides whose sequence was determined, 720 belong to the structural gene of SR-I. In the 5' non-coding region two putative promoter elements and a ribosomal binding site have been identified. The 3' flanking region bears a potent...

Journal: :Journal of chemical theory and computation 2007
Kazuhiro Fujimoto Shigehiko Hayashi Jun-Ya Hasegawa Hiroshi Nakatsuji

The excited states of the three retinal proteins, bovine rhodopsin (Rh), bacteriorhodopsin (bR), and sensory rhodopsin II (sRII) were studied using the symmetry-adapted cluster-configuration interaction (SAC-CI) and combined quantum mechanical and molecular mechanical (QM/MM) methods. The computed absorption energies are in good agreement with the experimental ones for all three proteins. The s...

Journal: :The Journal of biological chemistry 1987
T Gulik-Krzywicki M Seigneuret J L Rigaud

An improved freeze-fracture electron microscope procedure has been developed and applied to the study of the association of bacteriorhodopsin in large proteoliposomes reconstituted by reverse-phase evaporation with egg lecithin. Due to the improved accuracy and resolution of this procedure, intramembrane particles, the diameter of which (4.5 nm) closely matched that of bacteriorhodopsin monomer...

Journal: :Biochimica et biophysica acta 1990
R R Birge

II. Structure and function of rhodopsin and bacteriorhodopsin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 294 A. Organization of the proteins in the membrane . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 296 B. The photobleaching sequence of rhodopsin . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 297 C. The photocycle of bact...

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