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Analysis of single gene multitrait effects in livestock by the use of Gibbs sampling

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Dobek A., Molinski M. K., Molinski K., Szydlowski S. M., Szydlowski M., Szwaczkowski S. T., Szwaczkowski T.
Journal of Applied Genetics
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2000
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vol. 41
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issue 4
275-283
EN
The paper presents a method of multivariate data analysis described by a model which involves fixed effects, additive polygenic individual effects and the effects of a major gene. To find the estimates of model parameters, the maximalisation of likelihood function method is applied. The maximum of likelihood function is computed by the use of the Gibbs sampling approach. In this approach, following the conditional posterior distributions, values of all unknown parameters are generated. On the basis of the obtained samples the marginal posterior densities as well as the estimates of fixed effects, gene frequency, genotypic values, major gene, polygenic and error (co)variances are calculated. A numerical example, supplemented to theoretical considerations, deals with data simulated according to the considered model.
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Primary Electron Transfer Reactions in Membrane-Bound Open and Closed Reaction Centers from Purple Bacterium Rhodobacter sphaeroides

100%
Gibasiewicz K., Pajzderska M., Karolczak J., Burdziński G., Dobek A., Jones M.
Acta Physica Polonica A
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2012
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vol. 122
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issue 2
263-268
EN
Most ultrafast transient absorption studies of primary electron transfer in reaction centers from purple bacteria have been performed in complexes isolated from their natural lipid membrane environment using detergent. In this contribution we present near-UV-vis transient absorption studies of reaction centers embedded in their natural membrane environment. The evolution of absorption spectra recorded with subpicosecond resolution and reflecting primarily electron transfer reactions has been compared to data obtained previously for isolated reaction centers. We conclude that the overall spectral evolution in both types of samples is similar, and the environment of the reaction center protein has only a minor effect on the primary electron transfer reactions. The differences between the two samples are explained in terms of different energetic levels (and their different temporal evolution) of the two initial charge separated states P^+B_A^- and P^+H_A^-, with P being the primary electron donor and B_A and H_A the two consecutive electron acceptors. Additionally, in the electric field generated by P^+H_A^-, B_A in membrane-bound reaction centers undergoes a stronger electrochromic shift than in isolated reaction centers.
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