52 resultados para Z score
em Doria (National Library of Finland DSpace Services) - National Library of Finland, Finland
Resumo:
The Baltic Sea is a unique environment that contains unique genetic populations. In order to study these populations on a genetic level basic molecular research is needed. The aim of this thesis was to provide a basic genetic resource for population genomic studies by de novo assembling a transcriptome for the Baltic Sea isopod Idotea balthica. RNA was extracted from a whole single adult male isopod and sequenced using Illumina (125bp PE) RNA-Seq. The reads were preprocessed using FASTQC for quality control, TRIMMOMATIC for trimming, and RCORRECTOR for error correction. The preprocessed reads were then assembled with TRINITY, a de Bruijn graph-based assembler, using different k-mer sizes. The different assemblies were combined and clustered using CD-HIT. The assemblies were evaluated using TRANSRATE for quality and filtering, BUSCO for completeness, and TRANSDECODER for annotation potential. The 25-mer assembly was annotated using PANNZER (protein annotation with z-score) and BLASTX. The 25-mer assembly represents the best first draft assembly since it contains the most information. However, this assembly shows high levels of polymorphism, which currently cannot be differentiated as paralogs or allelic variants. Furthermore, this assembly is incomplete, which could be improved by sampling additional developmental stages.
Resumo:
The protein Ezrin, is a member of the ERM family (Ezrin, Radixin and Moesin) that links the F-actin to the plasma membrane. The protein is made of three domains namely the FERM domain, a central α-helical domain and the CERMAD domain. The residues in Ezrin such as Ser66, Tyr145, Tyr353 and Tyr477 regulate the function of the protein through phosphorylation. The protein is found in two distinct conformations of active and dormant (inactive) state. The initial step during the conformation change is the breakage of intramolecular interaction in dormant Ezrin by phosphorylation of residue Thr567. The dormant structure of human Ezrin was predicted computationally since only partial active form structure was available. The validation analysis showed that 99.7% residues were positioned in favored, allowed and generously allowed regions of the Ramachandran plot. The Z-score of Ezrin was −7.36, G-factor was 0.1, and the QMEAN score of the model was 0.61 indicating a good model for human Ezrin. The comparison of the conformations of the activated and dormant Ezrin showed a major shift in the F2 lobe (residues 142-149 and 161-177) while changes in the conformation induced mobility shifts in lobe F3 (residues 261 to 267). The 3D positions of the phosphorylation sites Tyr145, Tyr353, Tyr477, Tyr482 and Thr567 were also located. Using targeted molecular dynamic simulation, the molecular movements during conformational change from active to dormant were visualized. The dormant Ezrin auto-inhibits itself by a head-to-tail interaction of the N-terminal and C-terminal residues. The trajectory shows the breakage of the interactions and mobility of the CERMAD domain away from the FERM domain. Protein docking and clustering analysis were used to predict the residues involved in the interaction between dormant Ezrin and mTOR. Residues Tyr477 and Tyr482 were found to be involved in interaction with mTOR.
Resumo:
Helsingfors : Wasenius & Co. [1853]
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1 Helsingfors : A. W. Gröndahl 1847
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Soitinnus: sekakuoro.
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Translated into Finnish by Joh. Bäckwall.
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Engraved illustrations are based on the original oil paintings of several Finnish artists: A. v. Becker, A. Edelfelt, R. W. Ekman, W. Holmberg, K. E. Jansson, O. Kleineh, J. Knutson, B. Lindholm, H. Munsterhjelm och B. Reinhold.
Resumo:
Engraved illustrations are based on the original oil paintings of several Finnish artists: A. v. Becker, A. Edelfelt, R. W. Ekman, W. Holmberg, K. E. Jansson, O. Kleineh, J. Knutson, B. Lindholm, H. Munsterhjelm och B. Reinhold.
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Translated into Finnish by Wihtori Peltonen.
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Fourth revised edition.
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Lithographs from: Johan Knutson, Magnus v. Wright, Lennart Forstén, Pehr Adolf Kruskopf, F. J. Westerling, Adolf Wilhelm Lindeström, and J. Boström, and two lithographs without the artistʼs name.
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Supplementum-osassa paljon tyhjiä välilehtiä.
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Nimeke- ja tekijätiedot nimiönkehyksissä