Results 1 to 10 of about 30,370 (300)

Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser

Science, 2018
Look fast Organisms from bacteria to humans sense and react to light. Proteins that contain the light-sensitive molecule retinal couple absorption of light to conformational changes that produce a signal or move ions across a membrane. Nogly et al.
Przemyslaw M Nogly, Tobias Weinert, Daniel James   +2 more
exaly   +2 more sources

Bacteriorhodopsin Folds through a Poorly Organized Transition State [PDF]

Journal of the American Chemical Society, 2014
The folding mechanisms of helical membrane proteins remain largely uncharted. Here we characterize the kinetics of bacteriorhodopsin folding and employ φ-value analysis to explore the folding transition state.
J. P. Schlebach, Nicholas B. Woodall, J. Bowie, Chiwook Park   +3 more
semanticscholar   +4 more sources

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

Nature Communications, 2020
How does chemistry scale in complexity to unerringly direct biological functions? Nass Kovacs et al. have shown that bacteriorhodopsin undergoes structural changes tantalizingly similar to the expected pathway even under excessive excitation.
R. Miller, O. Paré-Labrosse, A. Sarracini, J. Besaw   +3 more
semanticscholar   +2 more sources

Bacteriorhodopsin of purple membrane reverses anisotropy outside the pH range of proton pumping based on logic gate realization. [PDF]

Sci Rep
The bacteriorhodopsin of purple membrane is the first discovered light-sensing protein among ion transporting microbial rhodopsins, some of which (e.g.
Mostafa HIA, Elfiki AA.
europepmc   +2 more sources

Single molecule kinetics of bacteriorhodopsin by HS-AFM [PDF]

Nature Communications, 2021
Here, the authors use high-speed atomic force microscopy (HS-AFM) methods to characterize the single molecule kinetics of wild-type bacteriorhodopsin (bR) with millisecond temporal resolution, providing new insights into the bR conformational cycle.
Alma P. Perrino, Atsushi Miyagi, Simon Scheuring   +2 more
doaj   +2 more sources

The Role of Graphene Monolayers in Enhancing the Yield of Bacteriorhodopsin Photostates for Optical Memory Applications [PDF]

Applied Sciences, 2021
Bacteriorhodopsin (bR) is a photoactive protein that has gained increasing importance as a tool for optical memory storage due to its remarkable photochemical and thermal stability.
Roma Patel, Gregory Salamone, Isaac Macwan   +2 more
doaj   +2 more sources

Reversible Photochromic Reactions of Bacteriorhodopsin from Halobacterium salinarum at Femto- and Picosecond Times. [PDF]

Molecules
The operation of bacteriorhodopsin (BR) from the archaeon Halobacterium salinarum is based on the photochromic reaction of isomerization of the chromophore group (the retinal protonated Schiff base, RPSB) from the all-trans to the 13-cis form.
Smitienko O, Feldman T, Shelaev I, Gostev F, Aybush A, Cherepanov D, Nadtochenko V, Ostrovsky M.   +7 more
europepmc   +2 more sources

Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct. [PDF]

Nat Commun
Discovered over 50 years ago, bacteriorhodopsin is the first recognized and most widely studied microbial retinal protein. Serving as a light-activated proton pump, it represents the archetypal ion-pumping system.
Malakar P, Gholami S, Aarabi M, Rivalta I, Sheves M, Garavelli M, Ruhman S.   +6 more
europepmc   +2 more sources

A three-dimensional movie of structural changes in bacteriorhodopsin

Science, 2016
Eriko Nango, Antoine Royant, Minoru Kubo
exaly   +2 more sources

High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin

Nature Nanotechnology, 2010
Mikihiro Shibata, Hayato Yamashita, Takayuki Uchihashi   +2 more
exaly   +2 more sources