نتایج جستجو برای: bacteriorhodopsin br

تعداد نتایج: 41878  

2011
Jonathan P. Schlebach Moon-Soo Kim Nathan H. Joh James U. Bowie Chiwook Park

In most cases authors are permitted to post their version of the article (e.g. in Word or Tex form) to their personal website or institutional repository. Authors requiring further information regarding Elsevier's archiving and manuscript policies are encouraged to visit: Technical challenges have greatly impeded the investigation of membrane protein folding and unfolding. To develop a new tool...

2009
Eric M. Winder Mark H. Griep Donald R. Lueking Craig R. Friedrich

This paper describes how monomeric bR can be overproduced in Escherichia coli and subsequently utilized as an integral component of a generic, nanoscale chemical sensing platform. The utility of this sensing platform is that it can be adapted for detection of a wide range of biological and chemical agents at, or below, nanomolar concentration levels. The gene encoding for bacteriorhodopsin has ...

Journal: :Nature nanotechnology 2010
Mikihiro Shibata Hayato Yamashita Takayuki Uchihashi Hideki Kandori Toshio Ando

Dynamic changes in protein conformation in response to external stimuli are important in biological processes, but it has proved difficult to directly visualize such structural changes under physiological conditions. Here, we show that high-speed atomic force microscopy can be used to visualize dynamic changes in stimulated proteins. High-resolution movies of a light-driven proton pump, bacteri...

Journal: :Bioengineered 2012
P Saeedi J Mohammadian Moosaabadi S Sina Sebtahmadi J Fallah Mehrabadi M Behmanesh S Mekhilef

Bacteriorhodopsin (BR), a model system in biotechnology, is a G-protein dependent trans membrane protein which serves as a light driven proton pump in the cell membrane of Halobacterium salinarum. Due to the linkage of retinal to the protein, it seems colored and has numbers of versatile properties. As in vitro culture of the Halobacteria is very difficult, and isolation is time consuming and u...

2009
Akira Kawanabe Hideki Kandori

Anabaena sensory rhodopsin (ASR) is an archaeal-type rhodopsin found in eubacteria. The gene encoding ASR forms a single operon with ASRT (ASR transducer) which is a 14 kDa soluble protein, suggesting that ASR functions as a photochromic sensor by activating the soluble transducer. This article reviews the detailed photoreaction processes of ASR, which were studied by low-temperature Fourier-tr...

Journal: :The Journal of biological chemistry 1984
M J Liao H G Khorana

Treatment of the purple membrane with carboxypeptidase A, Pronase, or papain, results in the cleavage of amino acids from the carboxyl terminus of bacteriorhodopsin, a maximum of about 17 amino acids being released with papain. Protease-treated bacteriorhodopsin, after denaturation, refolds to the native structure, binds retinal as tightly as the intact protein and, on reconstitution into vesic...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1993
S I Bibikov R N Grishanin A D Kaulen W Marwan D Oesterhelt V P Skulachev

The bacterio-opsin gene was introduced into a "blind" Halobacterium salinarium mutant that (i) lacked all the four retinal proteins [bacteriorhodopsin (BR), halorhodopsin, and sensory rhodopsins (SRs) I and II] and the transducer protein for SRI and (ii) showed neither attractant response to long wavelength light nor repellent response to short wavelength light. The resulting transformed cells ...

2015
Hideki Kandori

Rhodopsins are light-sensing proteins used in optogenetics. The word "rhodopsin" originates from the Greek words "rhodo" and "opsis," indicating rose and sight, respectively. Although the classical meaning of rhodopsin is the red-colored pigment in our eyes, the modern meaning of rhodopsin encompasses photoactive proteins containing a retinal chromophore in animals and microbes. Animal and micr...

Journal: :Biophysical journal 2002
Masayuki Iwamoto Yuji Furutani Yuki Sudo Kazumi Shimono Hideki Kandori Naoki Kamo

Pharaonis phoborhodopsin (ppR; also pharaonis sensory rhodopsin II, psRII) is a receptor of the negative phototaxis of Natronobacterium pharaonis. By spectroscopic titration of D193N and D193E mutants, the pK(a) of the Schiff base was evaluated. Asp193 corresponds to Glu204 of bacteriorhodopsin (bR). The pK(a) of the Schiff base (SBH(+)) of D193N was approximately 10.1-10.0 (at XH(+)) and appro...

Journal: :Protein engineering 1997
S L Lin B Yan

A structural model is constructed for the integral membrane protein, sensory rhodopsin I (SRI), the phototaxis receptor of the archaeon Halobacterium salinarium. The model is built on the template of the homologous bacteriorhodopsin (BR). The modeling procedure includes sequence alignment, a side chain rotamer search and simulated annealing by restricted molecular dynamics. The structure is in ...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید