Relevant bibliographies by topics / Rhodopsin proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Rhodopsin proteins'

Author: Grafiati
Published: 14 March 2023

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Journal articles on the topic "Rhodopsin proteins"

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Meng, Chao Luo, Gang Dai, and Tatsuo Iwasa. "Identification of Microbial Rhodopsin Genes from Salt Lake in Inner Mongolia." Advanced Materials Research 518-523 (May 2012): 380–83. http://dx.doi.org/10.4028/www.scientific.net/amr.518-523.380.

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Microbial rhodopsins are photoactive proteins that use retinal molecule as the photoactive center. Because of the structural simplicity and functional diversity, microbial rhodopsins have been an excellent model system for structural biology. In the past decades microbial rhodopisns were identified from diverse environments including salt lakes, fresh water, sea water, human and plant tissues as fungal pathogens. In the present work, we tried to identify microbial rhodopsin genes from salt lake in Inner Mongolia, China. Two bacteriorhodopsin-like genes were identified. The retrieved sequences
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Shen, Libing, Chao Chen, Hongxiang Zheng, and Li Jin. "The Evolutionary Relationship between Microbial Rhodopsins and Metazoan Rhodopsins." Scientific World Journal 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/435651.

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Rhodopsins are photoreceptive proteins with seven-transmembrane alpha-helices and a covalently bound retinal. Based on their protein sequences, rhodopsins can be classified into microbial rhodopsins and metazoan rhodopsins. Because there is no clearly detectable sequence identity between these two groups, their evolutionary relationship was difficult to decide. Through ancestral state inference, we found that microbial rhodopsins and metazoan rhodopsins are divergently related in their seven-transmembrane domains. Our result proposes that they are homologous proteins and metazoan rhodopsins or
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Tam, Beatrice M., Orson L. Moritz, Lawrence B. Hurd, and David S. Papermaster. "Identification of an Outer Segment Targeting Signal in the Cooh Terminus of Rhodopsin Using Transgenic Xenopus laevis." Journal of Cell Biology 151, no. 7 (2000): 1369–80. http://dx.doi.org/10.1083/jcb.151.7.1369.

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Mislocalization of the photopigment rhodopsin may be involved in the pathology of certain inherited retinal degenerative diseases. Here, we have elucidated rhodopsin's targeting signal which is responsible for its polarized distribution to the rod outer segment (ROS). Various green fluorescent protein (GFP)/rhodopsin COOH-terminal fusion proteins were expressed specifically in the major red rod photoreceptors of transgenic Xenopus laevis under the control of the Xenopus opsin promoter. The fusion proteins were targeted to membranes via lipid modifications (palmitoylation and myristoylation) as
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Fu, Hsu-Yuan, Yu-Cheng Lin, Yung-Ning Chang, et al. "A Novel Six-Rhodopsin System in a Single Archaeon." Journal of Bacteriology 192, no. 22 (2010): 5866–73. http://dx.doi.org/10.1128/jb.00642-10.

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ABSTRACT Microbial rhodopsins, a diverse group of photoactive proteins found in Archaea, Bacteria, and Eukarya, function in photosensing and photoenergy harvesting and may have been present in the resource-limited early global environment. Four different physiological functions have been identified and characterized for nearly 5,000 retinal-binding photoreceptors, these being ion transporters that transport proton or chloride and sensory rhodopsins that mediate light-attractant and/or -repellent responses. The greatest number of rhodopsins previously observed in a single archaeon had been four
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Poupault, Clara, Diane Choi, Khanh Lam-Kamath, et al. "A combinatorial cis-regulatory logic restricts color-sensing Rhodopsins to specific photoreceptor subsets in Drosophila." PLOS Genetics 17, no. 6 (2021): e1009613. http://dx.doi.org/10.1371/journal.pgen.1009613.

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Color vision in Drosophila melanogaster is based on the expression of five different color-sensing Rhodopsin proteins in distinct subtypes of photoreceptor neurons. Promoter regions of less than 300 base pairs are sufficient to reproduce the unique, photoreceptor subtype-specific rhodopsin expression patterns. The underlying cis-regulatory logic remains poorly understood, but it has been proposed that the rhodopsin promoters have a bipartite structure: the distal promoter region directs the highly restricted expression in a specific photoreceptor subtype, while the proximal core promoter regio
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Chuang, Jen-Zen, and Ching-Hwa Sung. "The Cytoplasmic Tail of Rhodopsin Acts as a Novel Apical Sorting Signal in Polarized MDCK Cells." Journal of Cell Biology 142, no. 5 (1998): 1245–56. http://dx.doi.org/10.1083/jcb.142.5.1245.

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All basolateral sorting signals described to date reside in the cytoplasmic domain of proteins, whereas apical targeting motifs have been found to be lumenal. In this report, we demonstrate that wild-type rhodopsin is targeted to the apical plasma membrane via the TGN upon expression in polarized epithelial MDCK cells. Truncated rhodopsin with a deletion of 32 COOH-terminal residues shows a nonpolar steady-state distribution. Addition of the COOH-terminal 39 residues of rhodopsin redirects the basolateral membrane protein CD7 to the apical membrane. Fusion of rhodopsin's cytoplasmic tail to a
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Tarlachkov, Sergey V., Taras V. Shevchuk, Maria del Carmen Montero-Calasanz, and Irina P. Starodumova. "Diversity of rhodopsins in cultivated bacteria of the family Geodermatophilaceae associated with non-aquatic environments." Bioinformatics 36, no. 6 (2019): 1668–72. http://dx.doi.org/10.1093/bioinformatics/btz840.

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Abstract Motivation A small amount of research is focused on investigation of rhodopsins in cultivated bacteria isolated from non-aquatic environments. Furthermore, the abundance of these proteins in strains from hot and arid habitats was not reported previously. Since there is an insignificant amount of such isolates, the enigmatic role of the rhodopsins in dry ecological niches is still poorly understood. The members of the family Geodermatophilaceae could be used as interesting objects to search for new rhodopsin genes that will provide novel insights into versatility and importance of thes
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Ahrendt, Steven R., Edgar Mauricio Medina, Chia-en A. Chang, and Jason E. Stajich. "Exploring the binding properties and structural stability of an opsin in the chytridSpizellomyces punctatususing comparative and molecular modeling." PeerJ 5 (April 27, 2017): e3206. http://dx.doi.org/10.7717/peerj.3206.

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BackgroundOpsin proteins are seven transmembrane receptor proteins which detect light. Opsins can be classified into two types and share little sequence identity: type 1, typically found in bacteria, and type 2, primarily characterized in metazoa. The type 2 opsins (Rhodopsins) are a subfamily of G-protein coupled receptors (GPCRs), a large and diverse class of seven transmembrane proteins and are generally restricted to metazoan lineages. Fungi use light receptors including opsins to sense the environment and transduce signals for developmental or metabolic changes. Opsins characterized in th
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Shtyrov, Andrey A., Dmitrii M. Nikolaev, Vladimir N. Mironov, et al. "Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima." International Journal of Molecular Sciences 22, no. 6 (2021): 3029. http://dx.doi.org/10.3390/ijms22063029.

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A typical feature of proteins from the rhodopsin family is the sensitivity of their absorption band maximum to protein amino acid composition. For this reason, studies of these proteins often require methodologies that determine spectral shift caused by amino acid substitutions. Generally, quantum mechanics/molecular mechanics models allow for the calculation of a substitution-induced spectral shift with high accuracy, but their application is not always easy and requires special knowledge. In the present study, we propose simple models that allow us to estimate the direct effect of a charged
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Konno, Masae, Yumeka Yamauchi, Keiichi Inoue, and Hideki Kandori. "Expression analysis of microbial rhodopsin-like genes in Guillardia theta." PLOS ONE 15, no. 12 (2020): e0243387. http://dx.doi.org/10.1371/journal.pone.0243387.

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The Cryptomonad Guillardia theta has 42 genes encoding microbial rhodopsin-like proteins in their genomes. Light-driven ion-pump activity has been reported for some rhodopsins based on heterologous E. coli or mammalian cell expression systems. However, neither their physiological roles nor the expression of those genes in native cells are known. To reveal their physiological roles, we investigated the expression patterns of these genes under various growth conditions. Nitrogen (N) deficiency induced color change in exponentially growing G. theta cells from brown to green. The 29 rhodopsin-like
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Dissertations / Theses on the topic "Rhodopsin proteins"

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Perera, Mahakumarage Suchithranga, and Mahakumarage Suchithranga Perera. "Investigation of Rhodopsin Activation Using Spectroscopic and Scattering Techniques." Diss., The University of Arizona, 2016. http://hdl.handle.net/10150/622975.

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G-protein–coupled receptors are the largest superfamily in the human genome, and involved in critical cellular signaling processes in living cells. Protein structural fluctuations are the key for GPCR function that is driven and modulated by a variety of factors that are not well understood. This dissertation focusses on understanding the activation of GPCRs using the visual receptor, rhodopsin as the prototype. Rhodopsin is an ideal candidate for this study, as it represents the largest class of GPCRs, and is known to demonstrate more noticeable structural changes upon activation compared
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Birkholz, Denise A. "Photoreceptor cell fate determination and rhodopsin expression in the developing eye of Drosophila /." Connect to full text via ProQuest. IP filtered, 2005.

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Farmer, Nicola Ann. "Folding and assembly of two alpha helical membrane proteins, rhodopsin and bacteriorhodopsin." Thesis, University of Bristol, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.402351.

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Murray, Anne Riché. "The functional significance of rhodopsin's N-linked glycosylation." Oklahoma City : [s.n.], 2009.

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Zhao, Xinyu. "Characterization of molecular forms of G protein-coupled receptor kinase 1 (rhodopsin kinase) in vertebrate retina and pineal gland /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/6259.

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Sapra, K. Tanuj. "Single-Molecule Measurements of Complex Molecular Interactions in Membrane Proteins using Atomic Force Microscopy." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2007. http://nbn-resolving.de/urn:nbn:de:swb:14-1175696409847-74867.

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Single-molecule force spectroscopy (SMFS) with atomic force microscope (AFM) has advanced our knowledge of the mechanical aspects of biological processes, and helped us take big strides in the hitherto unexplored areas of protein (un)folding. One such virgin land is that of membrane proteins, where the advent of AFM has not only helped to visualize the difficult to crystallize membrane proteins at the single-molecule level, but also given a new perspective in the understanding of the interplay of molecular interactions involved in the construction of these molecules. My PhD work was tightly fo
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Tomasello, Gaia <1981&gt. "Theoretical insight into the properties of light induced events of photochromic systems and rhodopsin proteins." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2009. http://amsdottorato.unibo.it/1726/1/Tomasello_Gaia_Tesi.pdf.

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Tomasello, Gaia <1981&gt. "Theoretical insight into the properties of light induced events of photochromic systems and rhodopsin proteins." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2009. http://amsdottorato.unibo.it/1726/.

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Sapra, K. Tanuj. "Single-Molecule Measurements of Complex Molecular Interactions in Membrane Proteins using Atomic Force Microscopy." Doctoral thesis, Technische Universität Dresden, 2006. https://tud.qucosa.de/id/qucosa%3A24922.

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Single-molecule force spectroscopy (SMFS) with atomic force microscope (AFM) has advanced our knowledge of the mechanical aspects of biological processes, and helped us take big strides in the hitherto unexplored areas of protein (un)folding. One such virgin land is that of membrane proteins, where the advent of AFM has not only helped to visualize the difficult to crystallize membrane proteins at the single-molecule level, but also given a new perspective in the understanding of the interplay of molecular interactions involved in the construction of these molecules. My PhD work was tightly fo
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Behnke, Craig A. "X-ray crystallographic analysis of three proteins : the novel structures of the corn Hageman factor inhibitor, the G-protein coupled receptor rhodopsin, and the ultra-high resolution structure of carbonic anhydrase /." Thesis, Connect to this title online; UW restricted, 2000. http://hdl.handle.net/1773/9206.

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Books on the topic "Rhodopsin proteins"

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Symposium on Rhodopsins and Phototransduction (1998 : Kyoto, Japan), ed. Rhodopsins and phototransduction. John Wiley, 1999.

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Biomolecular electronics: An introduction via photosensitive proteins. Birkhäuser, 1998.

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Jean-Louis, Rigaud, and Institut national de la santé et de la recherche médicale (France), eds. Structures and functions of retinal proteins: Proceedings of the Vth International Conference on Retinal Proteins held in Dourdan (France) June 28-July 3, 1992. INSERM, 1992.

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1942-1985, Eisenstein Laura, Ebrey Thomas G, and University of Illinois at Urbana-Champaign. Dept. of Physics., eds. Biophysical studies of retinal proteins: Proceedings of a conference in memory of Laura Eisenstein, held at Allerton Park Conference Center of the University of Illinois at Urbana-Champaign. Dept. of Physics, University of Illinois at Urbana-Champaign, 1987.

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L, Caron Marc, National Heart, Lung, and Blood Institute, and American Heart Association, eds. Receptors and cell activation: A summary of the Frontiers in Basic Sciences That Relate to Heart, Lung, and Blood Diseases Symposium : National Heart, Lung, and Blood Institute : administrative report. The Institute, 1987.

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Rees, Douglas C. Membrane Proteins (Advances in Protein Chemistry, Volume 63) (Advances in Protein Chemistry). Academic Press, 2003.

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Rees, Douglas C. Membrane Proteins. Elsevier Science & Technology Books, 2003.

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Membrane proteins. Academic Press, 2003.

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Rhodopsins and Phototransduction. John Wiley & Sons, 2000.

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Ovchinnikov, Yu A. Retinal Proteins: Proceedings of the International Conference, Ussr, 1986. Brill Academic Publishers, 1987.

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Book chapters on the topic "Rhodopsin proteins"

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González, Laura Pedraza, Leonardo Barneschi, Daniele Padula, Luca De Vico, and Massimo Olivucci. "Evolution of the Automatic Rhodopsin Modeling (ARM) Protocol." In Topics in Current Chemistry Collections. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-07658-9_5.

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AbstractIn recent years, photoactive proteins such as rhodopsins have become a common target for cutting-edge research in the field of optogenetics. Alongside wet-lab research, computational methods are also developing rapidly to provide the necessary tools to analyze and rationalize experimental results and, most of all, drive the design of novel systems. The Automatic Rhodopsin Modeling (ARM) protocol is focused on providing exactly the necessary computational tools to study rhodopsins, those being either natural or resulting from mutations. The code has evolved along the years to finally provide results that are reproducible by any user, accurate and reliable so as to replicate experimental trends. Furthermore, the code is efficient in terms of necessary computing resources and time, and scalable in terms of both number of concurrent calculations as well as features. In this review, we will show how the code underlying ARM achieved each of these properties.
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Fujita, Jun, Norika Sakurai, and Takao Shinozawa. "Presence of rhodopsin-like proteins in the planarian head." In Turbellarian Biology. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-2775-2_14.

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Chabre, M., and M. L. Applebury. "Interaction of Photoactivated Rhodopsin with Photoreceptor Proteins: The cGMP Cascade." In The Molecular Mechanism of Photoreception. Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70444-4_4.

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Durbeej, Bo. "A Computational Perspective on the Photochemistry of Photosensory Proteins: Phytochromes and Anabaena Sensory Rhodopsin." In Quantum Simulations of Materials and Biological Systems. Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4948-1_10.

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Ryba, Nicholas J. P., Matthew D. Hall, and John B. C. Findlay. "Rhodopsin." In Molecular Biology of G-Protein-Coupled Receptors. Birkhäuser Boston, 1992. http://dx.doi.org/10.1007/978-1-4684-6772-7_1.

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Deretic, Dusanka, and David S. Papermaster. "Low Molecular Weight GTP-binding Proteins Associated with the Membranes Involved in Post-Golgi Transport of Rhodopsin." In Molecular Mechanisms of Membrane Traffic. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_86.

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Gautier, Antoine, and Daniel Nietlispach. "Solution NMR Studies of Integral Polytopic α-Helical Membrane Proteins: The Structure Determination of the Seven-Helix Transmembrane Receptor Sensory Rhodopsin II, pSRII." In Membrane Protein Structure and Dynamics. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-023-6_3.

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Hofmann, K. P. "Rhodopsin/G-Protein Interaction." In GTPases in Biology II. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78345-6_17.

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Findlay, J. B. C. "Rhodopsin and G-Protein Linked Receptors." In Methods in Protein Sequence Analysis. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73834-0_67.

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Kandori, Hideki. "Protein-Controlled Isomerization in Rhodopsins". У Chemical Science of π-Electron Systems. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55357-1_41.

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Conference papers on the topic "Rhodopsin proteins"

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GUALTIERI, PAOLO. "RHODOPSIN-LIKE PROTEINS: THE UNIVERSAL AND PROBABLY UNIQUE PROTEINS FOR VISION." In Proceedings of the International School of Biophysics. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812799975_0002.

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Yu, Yunzhu, and Yuge Tong. "The evolutionary relationship of rhodopsin proteins across species." In International Conference on Biomedical and Intelligent Systems (IC-BIS 2022), edited by Ahmed El-Hashash. SPIE, 2022. http://dx.doi.org/10.1117/12.2660522.

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Hamm, P., M. Zurek, and T. Röschinger. "Femtosecond VIS and mid-IR Spectroscopy of the Photoisomerisation of Retinal." In International Conference on Ultrafast Phenomena. Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.tue.24.

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The light induced isomerisation of the retinal molecule (more exactly protonated Schiff base retinal, PSBR) plays an essential role in a number of important functional biomolecules like rhodopsin (responsible for vision), bacteriorhodopsin (BR, photosynthetic light induced proton pump) and halorhodopsin (HR, light induced chloride pump). These proteins were investigated in detail by femtosecond spectroscopy. In all cases, a fast S1 reaction occurs prior to the transition to the ground state. However, the details of the photoreaction critically depend on the specific surrounding of the chromoph
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Lutz, I. G., A. O. Sieg, J. Wachtveitl, et al. "Primary Reactions of Sensory Rhodopsin I and II: Two proteins with vastly different dynamics." In International Conference on Ultrafast Phenomena. OSA, 2000. http://dx.doi.org/10.1364/up.2000.wa6.

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Mukherjee, Rudranarayan M., Paul Crozier, and Kurt S. Anderson. "Multibody Molecular Dynamics II: Applications and Results." In ASME 2007 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/detc2007-35561.

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This is the second paper in a series of two papers on using multibody dynamics algorithms and methods for coarse grained molecular dynamics simulations. In the previous paper, the theoretical discussions on this topic have been presented. This paper presents results obtained from simulating several biomolecular and bulk materials using multibody dynamics algorithms. The systems studied include water boxes, alkane chains, alanine dipeptide and carboxyl terminal fragments of Calmodulin, Ribosomal, and Rhodopsin proteins. The atomistic representations of these systems include several thousand deg
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Zhong, Q., S. Ruhman, M. Ottolenghi, et al. "A Comparative Study of the Initial Photoinduced Event in Bacteriorhodopsin: Can it be Isomerization?" In International Conference on Ultrafast Phenomena. Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.pdp.5.

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Rhodopsins are a family of photoactivated 7 α-helix membrane proteins which play central roles in visual-transduction and bacterial photosynthesis. They share the same chromophore: A retinal polyene bound to the protein via a protonated Schiff base linkage. A comprehensive description of the molecular mechanism of light energy conversion in rhodopsins requires a detailed understanding of the primary photophysical events.
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Hofmann, Klaus P. "Visual process in retinal photoreceptors: analysis by intrinsic light scattering signals." In OSA Annual Meeting. Optica Publishing Group, 1989. http://dx.doi.org/10.1364/oam.1989.wd1.

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The rod photoreceptor of the retina is a quantum detector whose physiological function in physically unfavorable conditions (body temperature, salt solution) is made possible by specific protein interactions. Photon energy is stored by the receptor protein rhodopsin (R) in a structurally transformed state. Activated R interacts with transducin (a G-protein or guanine nucleotide binding protein). This catalyses binding to G of energy-rich nucleotide which in turn releases G in an activated form. Absorption of one photon leads to the activation of 1000 G in 1 s. Analogous relay systems are found
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Altoè, Piero, Marco Stenta, Marco Garavelli, Theodore E. Simos, and George Maroulis. "Rhodopsin and GFP Chromophores: QM∕MM Absorption Spectra in Solvent and Protein." In COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836178.

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Kholmurodov, Kholmirzo T., Yu E. Penionzhkevich, and E. A. Cherepanov. "Computer Molecular Dynamics Studies on Protein Structures (Visual Pigment Rhodopsin and Cyclin-Dependent Kinases)." In INTERNATIONAL SYMPOSIUM ON EXOTIC NUCLEI. AIP, 2007. http://dx.doi.org/10.1063/1.2746628.

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Reports on the topic "Rhodopsin proteins"

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Rafaeli, Ada, Russell Jurenka, and Chris Sander. Molecular characterisation of PBAN-receptors: a basis for the development and screening of antagonists against Pheromone biosynthesis in moth pest species. United States Department of Agriculture, 2008. http://dx.doi.org/10.32747/2008.7695862.bard.

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The original objectives of the approved proposal included: (a) The determination of species- and tissue-specificity of the PBAN-R; (b) the elucidation of the role of juvenile hormone in gene regulation of the PBAN-R; (c) the identificationof the ligand binding domains in the PBAN-R and (d) the development of efficient screening assays in order to screen potential antagonists that will block the PBAN-R. Background to the topic: Moths constitute one of the major groups of pest insects in agriculture and their reproductive behavior is dependent on chemical communication. Sex-pheromone blends are
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