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Relevant bibliographies by topics / Pigment proteine complexe

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Academic literature on the topic 'Pigment proteine complexe'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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Journal articles on the topic "Pigment proteine complexe"

1

Luciński, Robert, and Grzegorz Jackowski. "The structure, functions and degradation of pigment-binding proteins of photosystem II." Acta Biochimica Polonica 53, no. 4 (November 14, 2006): 693–708. http://dx.doi.org/10.18388/abp.2006_3297.

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Eleven proteins belonging to photosystem II (PSII) bind photosynthetic pigments in the form of thylakoid membrane-associated pigment-protein complexes. Five of them (PsbA, PsbB, PsbC, PsbD and PsbS) are assigned to PSII core complex while the remaining six (Lhcb1, Lhcb2, Lhcb3, Lhcb4, Lhcb5 and Lhcb6) constitute, along with their pigments, functional complexes situated more distantly with regard to P680 - the photochemical center of PSII. The main function of the pigment-binding proteins is to harvest solar energy and deliver it, in the form of excitation energy, ultimately to P680 although individual pigment-proteins may be engaged in other photosynthesis-related processes as well. The aim of this review is to present the current state of knowledge regarding the structure, functions and degradation of this family of proteins.

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Wang, Quan, and W. E. Moerner. "Dissecting pigment architecture of individual photosynthetic antenna complexes in solution." Proceedings of the National Academy of Sciences 112, no. 45 (October 5, 2015): 13880–85. http://dx.doi.org/10.1073/pnas.1514027112.

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Oligomerization plays a critical role in shaping the light-harvesting properties of many photosynthetic pigment−protein complexes, but a detailed understanding of this process at the level of individual pigments is still lacking. To study the effects of oligomerization, we designed a single-molecule approach to probe the photophysical properties of individual pigment sites as a function of protein assembly state. Our method, based on the principles of anti-Brownian electrokinetic trapping of single fluorescent proteins, step-wise photobleaching, and multiparameter spectroscopy, allows pigment-specific spectroscopic information on single multipigment antennae to be recorded in a nonperturbative aqueous environment with unprecedented detail. We focus on the monomer-to-trimer transformation of allophycocyanin (APC), an important antenna protein in cyanobacteria. Our data reveal that the two chemically identical pigments in APC have different roles. One (α) is the functional pigment that red-shifts its spectral properties upon trimer formation, whereas the other (β) is a “protective” pigment that persistently quenches the excited state of α in the prefunctional, monomer state of the protein. These results show how subtleties in pigment organization give rise to functionally important aspects of energy transfer and photoprotection in antenna complexes. The method developed here should find immediate application in understanding the emergent properties of other natural and artificial light-harvesting systems.

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Deravi, Leila F., Andrew P. Magyar, Sean P. Sheehy, George R. R. Bell, Lydia M. Mäthger, Stephen L. Senft, Trevor J. Wardill, et al. "The structure–function relationships of a natural nanoscale photonic device in cuttlefish chromatophores." Journal of The Royal Society Interface 11, no. 93 (April 6, 2014): 20130942. http://dx.doi.org/10.1098/rsif.2013.0942.

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Cuttlefish, Sepia officinalis , possess neurally controlled, pigmented chromatophore organs that allow rapid changes in skin patterning and coloration in response to visual cues. This process of adaptive coloration is enabled by the 500% change in chromatophore surface area during actuation. We report two adaptations that help to explain how colour intensity is maintained in a fully expanded chromatophore when the pigment granules are distributed maximally: (i) pigment layers as thin as three granules that maintain optical effectiveness and (ii) the presence of high-refractive-index proteins—reflectin and crystallin—in granules. The latter discovery, combined with our finding that isolated chromatophore pigment granules fluoresce between 650 and 720 nm, refutes the prevailing hypothesis that cephalopod chromatophores are exclusively pigmentary organs composed solely of ommochromes. Perturbations to granular architecture alter optical properties, illustrating a role for nanostructure in the agile, optical responses of chromatophores. Our results suggest that cephalopod chromatophore pigment granules are more complex than homogeneous clusters of chromogenic pigments. They are luminescent protein nanostructures that facilitate the rapid and sophisticated changes exhibited in dermal pigmentation.

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Takeuchi, TS, and JP Thornber. "Heat-Induced Alterations in Thylakoid Membrane Protein Composition in Barley." Functional Plant Biology 21, no. 6 (1994): 759. http://dx.doi.org/10.1071/pp9940759.

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Biochemical and spectroscopic studies on the effects of high temperatures (45-47� C) over a 1 h period on the protein composition, fluorescence and photochemical activities of the barley thylakoid membrane were made. Photosystem II (PS II) activity decreased as expected, and photosystem I (PS I) activity also unexpectedly decreased. Our data support previous conclusions that the decrease in PS I activity is largely due to inactivation (or loss) of a component between the two photosystems. A two-dimensional electrophoretic system permitted first the separation of the thylakoid pigment-protein complexes of unstressed and stressed plants, followed by a determination of their subunit composition. The changes in the protein composition of each pigment-protein complex in response to elevated temperatures were monitored. Heat changed the quaternary structure of PS II and resulted in removal of the oxygen-evolving enhancer proteins from the thylakoid, but did essentially no damage to the PS I complex. The PS II core complex dissociated from a dimeric form to a monomeric one, and the major LHC II component (LHC IIb) changed from a trimeric to a monomeric form. The pigments that are lost from thylakoids during heat stress are mainly removed from the PS II pigment-proteins.

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Carpentier, Robert, Roger M. Leblanc, and Guy Bellemare. "Chlorophyll Photobleaching in Pigment-Protein Complexes." Zeitschrift für Naturforschung C 41, no. 3 (March 1, 1986): 284–90. http://dx.doi.org/10.1515/znc-1986-0307.

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Pigment photobleaching was performed in thylakoid membranes of Hordeum vulgare (wild type, mutant Chlorina f2, Norfluranzon treated seedlings) and in pigment-protein complexes (CP-I and LHCP) isolated from H. vulgare and Chlamydomonas reinhardtii. Multiphasic kinetics were obtained in all of the above cases. Energy transfer towards pigments absorbing at longer wavelength is postulated as a general protection mechanism against photobleaching. This mechanism explains a substantial bleaching of carotenoids and a faster bleaching of chlorophyll aggregates, absorbing at long wavelength. These conclusions were valid for isolated complexes as well as for thylakoid membranes, although membranes were less sensitive to light.

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De Vico, Luca, André Anda, Vladimir Al Osipov, Anders Ø. Madsen, and Thorsten Hansen. "Macrocycle ring deformation as the secondary design principle for light-harvesting complexes." Proceedings of the National Academy of Sciences 115, no. 39 (September 7, 2018): E9051—E9057. http://dx.doi.org/10.1073/pnas.1719355115.

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Natural light-harvesting is performed by pigment–protein complexes, which collect and funnel the solar energy at the start of photosynthesis. The identity and arrangement of pigments largely define the absorption spectrum of the antenna complex, which is further regulated by a palette of structural factors. Small alterations are induced by pigment–protein interactions. In light-harvesting systems 2 and 3 from Rhodoblastus acidophilus, the pigments are arranged identically, yet the former has an absorption peak at 850 nm that is blue-shifted to 820 nm in the latter. While the shift has previously been attributed to the removal of hydrogen bonds, which brings changes in the acetyl moiety of the bacteriochlorophyll, recent work has shown that other mechanisms are also present. Using computational and modeling tools on the corresponding crystal structures, we reach a different conclusion: The most critical factor for the shift is the curvature of the macrocycle ring. The bending of the planar part of the pigment is identified as the second-most important design principle for the function of pigment–protein complexes—a finding that can inspire the design of novel artificial systems.

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Krüger, Tjaart P. J., Pavel Malý, Maxime T. A. Alexandre, Tomáš Mančal, Claudia Büchel, and Rienk van Grondelle. "How reduced excitonic coupling enhances light harvesting in the main photosynthetic antennae of diatoms." Proceedings of the National Academy of Sciences 114, no. 52 (December 11, 2017): E11063—E11071. http://dx.doi.org/10.1073/pnas.1714656115.

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Strong excitonic interactions are a key design strategy in photosynthetic light harvesting, expanding the spectral cross-section for light absorption and creating considerably faster and more robust excitation energy transfer. These molecular excitons are a direct result of exceptionally densely packed pigments in photosynthetic proteins. The main light-harvesting complexes of diatoms, known as fucoxanthin–chlorophyll proteins (FCPs), are an exception, displaying surprisingly weak excitonic coupling between their chlorophyll (Chl) a’s, despite a high pigment density. Here, we show, using single-molecule spectroscopy, that the FCP complexes of Cyclotella meneghiniana switch frequently into stable, strongly emissive states shifted 4–10 nm toward the red. A few percent of isolated FCPa complexes and ∼20% of isolated FCPb complexes, on average, were observed to populate these previously unobserved states, percentages that agree with the steady-state fluorescence spectra of FCP ensembles. Thus, the complexes use their enhanced sensitivity to static disorder to increase their light-harvesting capability in a number of ways. A disordered exciton model based on the structure of the main plant light-harvesting complex explains the red-shifted emission by strong localization of the excitation energy on a single Chl a pigment in the terminal emitter domain due to very specific pigment orientations. We suggest that the specific construction of FCP gives the complex a unique strategy to ensure that its light-harvesting function remains robust in the fluctuating protein environment despite limited excitonic interactions.

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Dymova, Olga, Mikhail Khristin, Zbigniew Miszalski, Andrzej Kornas, Kazimierz Strzalka, and Tamara Golovko. "Seasonal variations of leaf chlorophyll–protein complexes in the wintergreen herbaceous plant Ajuga reptans L." Functional Plant Biology 45, no. 5 (2018): 519. http://dx.doi.org/10.1071/fp17199.

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The chlorophyll and carotenoid content, and the spectra of low-temperature fluorescence of the leaves, chloroplasts and isolated pigment–protein complexes in the perennial herbaceous wintergreen plant Ajuga reptans L. (bugle) in different seasons of the year were studied. During winter, these plants downregulate photosynthesis and the PSA is reorganised, including the loss of chlorophyll, possible reductions in the number of functional reaction centres of PSII, and changes in aggregation of the thylakoid protein complexes. We also observed a restructuring of the PSI–PSII megacomplex and the PSII–light-harvesting complex II supercomplex in leaves covered by snow. After snowmelt, the monomeric form of the chl a/b pigment–protein complex associated with PSII (LHCII) and the free pigments were also detected. We expect that snow cover provides favourable conditions for keeping photosynthetic machinery ready for photosynthesis in spring just after snowmelt. During winter, the role of the zeaxanthin-dependent protective mechanism, which is responsible for the dissipation of excess absorbed light energy, is likely to increase.

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Lehto, Kirsi, Mikko Tikkanen, Jean-Baptiste Hiriart, Virpi Paakkarinen, and Eva-Mari Aro. "Depletion of the Photosystem II Core Complex in Mature Tobacco Leaves Infected by the Flavum Strain of Tobacco mosaic virus." Molecular Plant-Microbe Interactions® 16, no. 12 (December 2003): 1135–44. http://dx.doi.org/10.1094/mpmi.2003.16.12.1135.

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The flavum strain of Tobacco mosaic virus (TMV) differs from the wild-type (wt) virus by causing strong yellow and green mosaic in the systemically infected developing leaves, yellowing in the fully expanded leaves, and distinct malformations of chloroplasts in both types of infected tissues. Analysis of the thylakoid proteins of flavum strain-infected tobacco leaves indicated that the chlorosis in mature leaves was accompanied by depletion of the entire photosystem II (PSII) core complexes and the 33-kDa protein of the oxygen evolving complex. The only change observed in the thyla-koid proteins of the corresponding wt TMV-infected leaves was a slight reduction of the α and β subunits of the ATP synthase complex. The coat proteins of different yellowing strains of TMV are known to effectively accumulate inside chloroplasts, but in this work, the viral movement protein also was detected in association with the thylakoid membranes of flavum strain-infected leaves. The mRNAs of different enzymes involved in the chlorophyll biosynthesis pathway were not reduced in the mature chlorotic leaves. These results suggest that the chlorosis was not caused by reduction of pigment biosynthesis, but rather, by reduction of specific proteins of the PSII core complexes and by consequent break-down of the pigments.

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Milivojevic, D. B., D. D. Stojanovic, and S. D. Drinic. "Effects of Aluminium on Pigments and Pigment-Protein Complexes of Soybean." Biologia plantarum 43, no. 4 (December 1, 2000): 595–97. http://dx.doi.org/10.1023/a:1002899932075.

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Dissertations / Theses on the topic "Pigment proteine complexe"

1

Robert, Bruno. "Etude de la structure et des interactions au sein des complexes proteine pigments impliques dans la photosynthese bacterienne : contribution de la spectrometrie raman de resonance." Paris 6, 1987. http://www.theses.fr/1987PA066603.

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Ebadati, Nasrollah D. "Characterization of the Pigment-Protein Complex in Corynebacterium Poinsettiae." Thesis, North Texas State University, 1986. https://digital.library.unt.edu/ark:/67531/metadc798269/.

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The purpose of this study was to completely characterize the protein moiety in the caroteno complex in C. poinsettae, determine if the distribution and level of protein in the pigment-protein complex in membranes of the wild type and in a colorless mutant could account for the differences in the stability of the membrane, and to determine if this protein is common to other pigmented and non-pigmented organisms. Also, electron microscopy of cell membranes of C. poinsettiae which had been exposed to gold-labelled antibody against the protein moitey of the pigment-protein complex, demonstrating that the protein is randomly distributed in the membranes of both wild type and colorless mutant.

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Joshua, Sarah. "Mobility of pigment-protein complexes in cyanobacteria." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1444430/.

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Phycobilisomes, the light harvesting complexes of cyanobacteria are highly mobile, fluorescent complexes known to diffuse freely on the thylakoid membranes, interacting with the reaction centre complexes to mediate efficient photosynthesis. The primary aim of this project is to establish what processes require this rapid movement of the complexes using a number of genetic, biochemical and microscopic techniques. The cyanobacterial species used extensively in the work presented in this thesis are the fully sequenced, naturally transformable Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7942. The latter lends itself particularly well to quantitatively elucidating the diffusion rate of fluorescent complexes, but qualitative detection of mobile fluorescent complex is also feasible with Synechocystis 6803. State transitions are observed in cyanobacteria upon the alteration of illumination conditions. A rapid redistribution of excitation energy between the reaction centres is observed. This was investigated using high osmotic strength buffers to fix phycobilisomes to reaction centres they were associating with upon their addition, thus inhibiting their mobility, as adjudged by spectroscopy and microscopy using the Fluorescence Recovery after Photobleaching (FRAP) technique. It was found that mobile phycobilisomes are required for cells to be capable of state transitions. Non-Photochemical Quenching (NPQ) is a protective mechanism seen in iron- deprived cyanobacteria. Extensively studied in plants, its supposed function is to dissipate excess energy as heat to prevent photodamage to the reaction centres. Using Synechocystis 6803 and the techniques described above, phycobilisome mobility was determined to be critical to NPQ induction, and the interaction with IsiA in cyanobacteria was proposed as being involved in the process. A previously inactivated gene thought to be involved in state transitions, rpaC, was over-expressed in Synechocystis 6803 and knocked out in Synechococcus 7942 and gave pleiotropic effects. The conclusion that the binding of phycobilisomes to PSII is predictably stronger than to PSI was exploited by comparing the strength of the binding in the Synechococcus 7942 mutant with the wild type. Data were suggestive of the protein being involved in phycobilisome to PSII binding. Psb28* mutants of both species used in this thesis were extensively characterised, as the cells also presented a highly unusual mobile PSII phenotype. Psb28 is possibly involved in maintaining thylakoid membrane organisation.

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Houlné, Guy. "Structure et expression des genes codant pour les apoproteines des antennes collectrices de photons ps2 et ps1 chez euglena gracilis." Université Louis Pasteur (Strasbourg) (1971-2008), 1988. http://www.theses.fr/1988STR13169.

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Hofmann, Clemens. "Pigment pigment interactions and protein dynamics in light harvesting complexes a single molecule study /." [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=971750483.

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Nieder, Jana Berit [Verfasser]. "Single-molecule spectroscopy on pigment-protein complexes / Jana Berit Nieder." Berlin : Freie Universität Berlin, 2011. http://d-nb.info/102593881X/34.

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Kell, Adam. "Energy transfer and exciton dynamics in photosynthetic pigment–protein complexes." Diss., Kansas State University, 2016. http://hdl.handle.net/2097/32539.

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Doctor of Philosophy
Chemistry
Ryszard J. Jankowiak
The structure-function relationships of natural pigment–protein complexes are of great interest, as the electronic properties of the pigments are tuned by the protein environment to achieve high quantum yields and photon utilization. Determination of electronic structure and exciton dynamics in protein complexes is complicated by static disorder and uncertainties in the properties of system-bath coupling. The latter is described by the phonon profile (or spectral density), whose shape can only be reliably measured experimentally for the lowest energy state. Low-temperature, laser-based spectroscopies are applied towards model pigment–protein complexes, i.e., the Fenna-Matthews-Olson (FMO) and water-soluble chlorophyll-binding (WSCP) complexes, in order to study system-bath coupling and energy transfer pathways. Site-selective techniques, e.g., hole burning (HB) and fluorescence line narrowing, are utilized to overcome static disorder and reveal details on homogeneous broadening. In addition, excitonic calculations with non-Markovian lineshapes provide information on electronic structure and exciton dynamics. A new lognormal functional form of the spectral density is recommended which appropriately defines electron-phonon parameters, i.e., Huang-Rhys factor and reorganization energy. Absorbance and fluorescence spectral shifts and HB spectra reveal that samples of FMO may contain a subpopulation of destabilized proteins with modified HB efficiencies. Simulations of spectra corresponding to intact proteins indicate that the entire trimer has to be taken into account in order to properly describe fluorescence and HB spectra. The redshifted fluorescence spectrum of WSCP is described by uncorrelated energy transfer as opposed to previous models of excited state protein relaxation. Also, based on nonconservative HB spectra measured for WSCP, a mechanism of electron transfer between chlorophylls and aromatic amino acids is proposed.

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Schmitt, Franz-Josef [Verfasser], and Hans Joachim [Akademischer Betreuer] Eichler. "Picobiophotonics for the investigation of pigment-pigment and pigment-protein interactions in photosynthetic complexes / Franz-Josef Schmitt. Betreuer: Hans Joachim Eichler." Berlin : Universitätsbibliothek der Technischen Universität Berlin, 2011. http://d-nb.info/1014971691/34.

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Adolphs, Julia [Verfasser]. "Theory of Excitation Energy Transfer in Pigment-Protein Complexes / Julian Adolphs." Berlin : Freie Universität Berlin, 2008. http://d-nb.info/1022719130/34.

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McDermott, Gerry. "Structural studies on an integral membrane light-harvesting complex." Thesis, University of Glasgow, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337507.

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Books on the topic "Pigment proteine complexe"

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Ravi, Sai Kishore, and Swee Ching Tan. Solar Energy Harvesting with Photosynthetic Pigment-Protein Complexes. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-6333-1.

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Dijk, Bastiaan van. Magnetic and electric field effects in photosynthetic pigment-protein complexes. Leiden: University of Leiden, 1998.

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Pigment–Protein Complexes in Plastids. Elsevier, 1993. http://dx.doi.org/10.1016/c2013-0-11562-0.

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Pigment-protein complexes in plastids: Synthesis and assembly. San Diego: Academic Press, 1993.

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Tan, Swee Ching, and Sai Kishore Ravi. Solar Energy Harvesting with Photosynthetic Pigment-Protein Complexes. Springer, 2020.

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Sundqvist, Christer. Pigment-Protein Complexes in Plastids: Synthesis and Assembly (Cell Biology). Academic Pr, 1993.

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Sundqvist, Christer. Pigment-Protein Complexes in Plastids: Synthesis and Assembly (Cell Biology). Academic Pr, 1993.

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Fawley, Marvin W. Biochemical and immunochemical studies of the light-harvesting pigment-protein complexes of algae. 1985.

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Book chapters on the topic "Pigment proteine complexe"

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Young, A. J. "Carotenoids in pigment-protein complexes." In Carotenoids in Photosynthesis, 72–95. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2124-8_3.

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Gruszecki, Wieslaw I. "Carotenoids in Pigment-Protein Complexes." In Carotenoids, 147–58. Chichester, UK: John Wiley & Sons, Ltd, 2016. http://dx.doi.org/10.1002/9781118622223.ch9.

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Ostroumov, Evgeny E., Yaser R. Khan, Gregory D. Scholes, and Govindjee. "Photophysics of Photosynthetic Pigment-Protein Complexes." In Advances in Photosynthesis and Respiration, 97–128. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-9032-1_4.

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Ryberg, M., N. Artus, B. Böddi, A. Lindsten, B. Wiktorsson, and C. Sundqvist. "Pigment-Protein Complexes of Chlorophyll Precursors." In Regulation of Chloroplast Biogenesis, 217–24. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3366-5_30.

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Knoetzel, J., I. Damm, and L. Rensing. "Pigment Composition of Pigment-Protein Complexes from the Dinoflagellate Gonyaulax Polyedra." In Progress in Photosynthesis Research, 137–40. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_33.

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Henges, Alexandra, and Peter Jahns. "Pigment Stoichiometries of Pigment-Protein Complexes from Pea (Pisum sativum): Localization of the Xanthophyll Cycle Pigments after Photoinhibitory Illumination." In Photosynthesis: from Light to Biosphere, 3031–34. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_710.

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Sperling, Ulrich, Geneviève Frick, Barbara Cleve, Klaus Apel, and Gregory A. Armstrong. "Pigment-Protein Complexes, Plastid Development and Photooxidative Protection." In The Chloroplast: From Molecular Biology to Biotechnology, 97–102. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4788-0_14.

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Ravi, Sai Kishore, and Swee Ching Tan. "Introduction." In Solar Energy Harvesting with Photosynthetic Pigment-Protein Complexes, 1–25. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-6333-1_1.

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Ravi, Sai Kishore, and Swee Ching Tan. "Augmenting Photocurrent Using Photoproteins of Complementary Optical Characteristics." In Solar Energy Harvesting with Photosynthetic Pigment-Protein Complexes, 27–40. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-6333-1_2.

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Ravi, Sai Kishore, and Swee Ching Tan. "Interfacing Photoproteins with Mechanoresponsive Electrolytes for Enhancing Photocurrent and Stability." In Solar Energy Harvesting with Photosynthetic Pigment-Protein Complexes, 41–64. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-6333-1_3.

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Conference papers on the topic "Pigment proteine complexe"

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Betke, Alexander, Bernd Voigt, Heiko Lokstein, and Ralf Menzel. "Two-photon fluorescence excitation spectroscopy of photosynthetic pigments and pigment-protein complexes." In 12th European Quantum Electronics Conference CLEO EUROPE/EQEC. IEEE, 2011. http://dx.doi.org/10.1109/cleoe.2011.5943251.

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Stoitchkova, Katerina, Atanaska Andreeva, Mira Busheva, Beverly Karplus Hartline, Renee K. Horton, and Catherine M. Kaicher. "Relation Between Changes in Pigments’ Spectral Properties and Structural Distortions of Pigment Protein Complexes (abstract)." In WOMEN IN PHYSICS: Third IUPAP International Conference on Women in Physics. AIP, 2009. http://dx.doi.org/10.1063/1.3137885.

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Köhler, J., A. M. van Oijen, M. Ketelaars, C. Hofmann, M. Matsushita, T. J. Aartsma, and J. Schmidt. "Optical Spectroscopy of Individual Photosynthetic Pigment Protein Complexes." In Proceedings of 2000 International Conference. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811387_0015.

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Gruszecki, Wieslaw I., Ewa Janik, Wojciech Grudzinski, Peter Kernen, Malgorzata Gospodarek, Waldemar Maksymiec, and Zbigniew Krupa. "Specific molecular aggregation of photosynthetic pigment-protein complex LHCII." In Biomedical Optics (BiOS) 2008, edited by Jörg Enderlein, Zygmunt K. Gryczynski, and Rainer Erdmann. SPIE, 2008. http://dx.doi.org/10.1117/12.761718.

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Ksenzenko, V. M., M. I. Molchanov, A. N. Tikhonov, and E. A. Zhukov. "The Detection, Isolation and Characterizaiton of Photosystem II Pigment-LIPID-Protein Complexes." In EQEC'96. 1996 European Quantum Electronic Conference. IEEE, 1996. http://dx.doi.org/10.1109/eqec.1996.561789.

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Lahav, Yigal, Ofer M. Shir, and Dror Noy. "Solving structures of pigment-protein complexes as inverse optimization problems using decomposition." In GECCO '17: Genetic and Evolutionary Computation Conference. New York, NY, USA: ACM, 2017. http://dx.doi.org/10.1145/3071178.3071197.

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Gil, Gabriel, Guido Goldoni, and Stefano Corni. "Enhanced light-harvesting of protein-pigment complexes assisted by a quantum dot antenna*." In 2018 Nanotechnology for Instrumentation and Measurement (NANOfIM). IEEE, 2018. http://dx.doi.org/10.1109/nanofim.2018.8688607.

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Purvis, Katherine, Kennedy Brittain, Ariana Joseph, Richard Cisek, and Danielle Tokarz. "Photosynthetic Pigments and Protein Complexes as Dyes For Third Harmonic Generation Microscopy." In 2019 Photonics North (PN). IEEE, 2019. http://dx.doi.org/10.1109/pn.2019.8819566.

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Grigoryeva, Natalia Y., and Sofia A. Ivanova. "Fluorescence spectroscopy and confocal microscopic spectroscopy for investigation of structure and functioning of natural pigment-protein complexes for biosensorics." In PROCEEDINGS OF INTERNATIONAL CONFERENCE ON RECENT TRENDS IN MECHANICAL AND MATERIALS ENGINEERING: ICRTMME 2019. AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0018501.

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Reports on the topic "Pigment proteine complexe"

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Buck, D. R. Theoretical Simulations and Ultrafast Pump-probe Spectroscopy Experiments in Pigment-protein Photosynthetic Complexes. Office of Scientific and Technical Information (OSTI), September 2000. http://dx.doi.org/10.2172/764683.

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