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You searched for subject:(Retinal analog). Showing records 1 – 3 of 3 total matches.

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1. Savedra, Ranylson Marcello Leal. Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada.

Degree: Mestrado, Físico-Química, 2008, University of São Paulo

As transições eletrônicas que apresenta as energias mais baixas no retinal e em quatro retinais sintéticos foram analisadas em dois diferentes ambientes: no vácuo e ligados à proteína bacterioopsina por uma base de Schiff protonada, utilizando diversos métodos de química teórica. Os resultados aqui apresentados fornecem indicativos de que três estados eletrônicos estão envolvidos na formação da primeira banda de absorção dos aldeídos, enquanto que, no caso dos compostos ligados à proteína apenas dois estados estariam envolvidos. As análises discutidas neste trabalho também sugerem uma possível explicação para o envolvimento de dois estados eletrônicos excitados no processo de fotoisomerização do retinal ligado à bacterioopsina.

Low-lying electronic transitions of retinal and of four synthetic retinals were analyzed in two different environments: in vacuum and linked to bacterioopsin through a protonated Schiff base, employing several methods of theoretical chemistry. The results here reported suggest that the first absorption band of the aldehydes involves three electronic states, while for the case of protein linked compounds, two states would be embraced. Our discussions also provided a possible explanation about the involvement of two electronic excited states in the photoisomerization process of retinal linked to bacterioopsin.

Advisors/Committee Members: Trsic, Milan.

Subjects/Keywords: all-trans-retinal; bacteriorhodopsin; bacteriorodopsina; QM/MM; QM/MM; retinais análogos; retinal analog; TDDFT; TDDFT; TDHF; TDHF; todo-trans-retinal; ZINDO/S-CI; ZINDO/S-CI

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APA (6th Edition):

Savedra, R. M. L. (2008). Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada. (Masters Thesis). University of São Paulo. Retrieved from http://www.teses.usp.br/teses/disponiveis/75/75131/tde-15092008-094453/ ;

Chicago Manual of Style (16th Edition):

Savedra, Ranylson Marcello Leal. “Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada.” 2008. Masters Thesis, University of São Paulo. Accessed September 24, 2020. http://www.teses.usp.br/teses/disponiveis/75/75131/tde-15092008-094453/ ;.

MLA Handbook (7th Edition):

Savedra, Ranylson Marcello Leal. “Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada.” 2008. Web. 24 Sep 2020.

Vancouver:

Savedra RML. Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada. [Internet] [Masters thesis]. University of São Paulo; 2008. [cited 2020 Sep 24]. Available from: http://www.teses.usp.br/teses/disponiveis/75/75131/tde-15092008-094453/ ;.

Council of Science Editors:

Savedra RML. Estudo de propriedades estruturais e eletrônicas de retinais e de retinais ligados à lisina via base de Schiff protonada. [Masters Thesis]. University of São Paulo; 2008. Available from: http://www.teses.usp.br/teses/disponiveis/75/75131/tde-15092008-094453/ ;


Kyoto University

2. Shen, Yi-Chung. Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore .

Degree: 2019, Kyoto University

Subjects/Keywords: channelrhodopsin; retinal analogue; spectra red-shift; C1C2; optogenetics

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APA (6th Edition):

Shen, Y. (2019). Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore . (Thesis). Kyoto University. Retrieved from http://hdl.handle.net/2433/242648

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Shen, Yi-Chung. “Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore .” 2019. Thesis, Kyoto University. Accessed September 24, 2020. http://hdl.handle.net/2433/242648.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Shen, Yi-Chung. “Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore .” 2019. Web. 24 Sep 2020.

Vancouver:

Shen Y. Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore . [Internet] [Thesis]. Kyoto University; 2019. [cited 2020 Sep 24]. Available from: http://hdl.handle.net/2433/242648.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Shen Y. Development of Red-Shifted Channelrhodopsin Variants Having Chemically Modified Retinylidene Chromophore . [Thesis]. Kyoto University; 2019. Available from: http://hdl.handle.net/2433/242648

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Leiden University

3. Ganapathy, S. Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps.

Degree: 2017, Leiden University

Microbial rhodopsins are photosensitive pigments implemented in the growth and adaptation of a large population of microorganisms. These relatively simple, tunable photosystems use a molecule of retinal as a chromophore to facilitate the conversion of sunlight to chemical energy. Retinal-based phototrophy is believed to sustain the phototrophic balance of various biospheres and has several important biotechnological applications. In this thesis, we propose the use of microbial rhodopsins as an alternative photosystem in a complementary approach towards more efficient use of photons in the solar spectrum. Towards this end, we describe the adaptation of two rhodopsin proton-pumps, namely proteorhodopsin and Gloeobacter rhodopsin, to shift their action spectrum into the near-infrared region. Several red-shifted variants of were generated by utilizing a combination of retinal analogs with specific opsin mutations. We also constructed a novel directed-evolution set-up, which allows us to generate a library of red-shifted mutants with simultaneous screening for spectral shifts and proton-pumping ability. Finally, the impact of a detergent or lipid microenvironment was tested on the various pigments generated in this study. Our results have important prospects in a number of biotechnological fields such as optogenetics, membrane-sensor technology and as a complementary photosystem for oxygenic photosynthesis. Advisors/Committee Members: Supervisor: Grip W.J. de, de, Groot H.J.M..

Subjects/Keywords: Phototrophy; Microbial rhodopsin; Proteorhodopsin; Proton pump; Spectral tuning; Retinal analog; Protein engineering; Mutagenesis; Directed evolution microenvironment; Phototrophy; Microbial rhodopsin; Proteorhodopsin; Proton pump; Spectral tuning; Retinal analog; Protein engineering; Mutagenesis; Directed evolution microenvironment

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Ganapathy, S. (2017). Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps. (Doctoral Dissertation). Leiden University. Retrieved from http://hdl.handle.net/1887/57985

Chicago Manual of Style (16th Edition):

Ganapathy, S. “Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps.” 2017. Doctoral Dissertation, Leiden University. Accessed September 24, 2020. http://hdl.handle.net/1887/57985.

MLA Handbook (7th Edition):

Ganapathy, S. “Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps.” 2017. Web. 24 Sep 2020.

Vancouver:

Ganapathy S. Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps. [Internet] [Doctoral dissertation]. Leiden University; 2017. [cited 2020 Sep 24]. Available from: http://hdl.handle.net/1887/57985.

Council of Science Editors:

Ganapathy S. Improvisations in phototrophy. Protein engineering and functional investigation of rhodopsin proton-pumps. [Doctoral Dissertation]. Leiden University; 2017. Available from: http://hdl.handle.net/1887/57985

.