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Structural Modeling (structural + modeling)
Selected AbstractsStructural Modeling of Car Use on the Way to the University in Different Settings: Interplay of Norms, Habits, Situational Restraints, and Perceived Behavioral Control,JOURNAL OF APPLIED SOCIAL PSYCHOLOGY, Issue 8 2009Christian A. Klöckner This manuscript presents the results of the application of an extended norm activation model to the explanation of car use on the way to the university with a sample of 430 students of 3 German universities. The proposed two-stage structural model is supported by the data. First, a norm activation process starting with awareness of consequences activates subjective and personal norms. Second, behavior is determined by car-use habits, perceived behavioral control (PBC), car access, and effort to use public transportation. The influence of personal norms on behavior is mediated by habits. Subgroup analyses of the second stage of the model show a high structural stability, but differences in the regression weights. [source] Bayesian strategy assessment in multi-attribute decision makingJOURNAL OF BEHAVIORAL DECISION MAKING, Issue 3 2003Arndt Bröder Abstract Behavioral Decision Research on multi-attribute decision making is plagued with the problem of drawing inferences from behavioral data on cognitive strategies. This bridging problem has been tackled by a range of methodical approaches, namely Structural Modeling (SM), Process Tracing (PT), and comparative model fitting. Whereas SM and PT have been criticized for a number of reasons, the comparative fitting approach has some theoretical advantages as long as the formal relation between theories and data is specified. A Bayesian method is developed that is able to assess, whether an empirical data vector was most likely generated by a ,Take The Best' heuristic (Gigerenzer et al., 1991), by an equal weight rule, or a compensatory strategy. Equations are derived for the two- and three-alternative cases, respectively, and a simulation study supports its validity. The classification also showed convergent validity with Process Tracing measures in an experiment. Potential extensions of the general approach to other applications in behavioral decision research are discussed. Copyright © 2003 John Wiley & Sons, Ltd. [source] Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesisFEBS JOURNAL, Issue 8 2008Camila A. O. Dias Eukaryotic translation initiation factor 5A (eIF5A) is a protein that is highly conserved and essential for cell viability. This factor is the only protein known to contain the unique and essential amino acid residue hypusine. This work focused on the structural and functional characterization of Saccharomyces cerevisiae eIF5A. The tertiary structure of yeast eIF5A was modeled based on the structure of its Leishmania mexicana homologue and this model was used to predict the structural localization of new site-directed and randomly generated mutations. Most of the 40 new mutants exhibited phenotypes that resulted from eIF-5A protein-folding defects. Our data provided evidence that the C-terminal ,-helix present in yeast eIF5A is an essential structural element, whereas the eIF5A N-terminal 10 amino acid extension not present in archaeal eIF5A homologs, is not. Moreover, the mutants containing substitutions at or in the vicinity of the hypusine modification site displayed nonviable or temperature-sensitive phenotypes and were defective in hypusine modification. Interestingly, two of the temperature-sensitive strains produced stable mutant eIF5A proteins , eIF5AK56A and eIF5AQ22H,L93F, and showed defects in protein synthesis at the restrictive temperature. Our data revealed important structural features of eIF5A that are required for its vital role in cell viability and underscored an essential function of eIF5A in the translation step of gene expression. [source] A novel FIP1L1-PDGFRA mutant destabilizing the inactive conformation of the kinase domain in chronic eosinophilic leukemia/hypereosinophilic syndromeALLERGY, Issue 6 2009S. Salemi Background:, The Fip1-like-1,platelet-derived growth factor receptor alpha (FIP1L1-PDGFRA) gene fusion is a common cause of chronic eosinophilic leukemia (CEL)/hypereosinophilic syndrome (HES), and patients suffering from this particular subgroup of CEL/HES respond to low-dose imatinib therapy. However, some patients may develop imatinib resistance because of an acquired T674I mutation, which is believed to prevent drug binding through steric hindrance. Methods:, In an imatinib resistant FIP1L1-PDGFRA positive patient, we analyzed the molecular structure of the fusion gene and analyzed the effect of several kinase inhibitors on FIP1L1-PDGFRA-mediated proliferative responses in vitro. Results:, Sequencing of the FIP1L1-PDGFRA fusion gene revealed the occurrence of a S601P mutation, which is located within the nucleotide binding loop. In agreement with the clinical observations, imatinib did not inhibit the proliferation of S601P mutant FIP1L1-PDGFRA-transduced Ba/F3 cells. Moreover, sorafenib, which has been described to inhibit T674I mutant FIP1L1-PDGFRA, failed to block S601P mutant FIP1L1-PDGFRA. Structural modeling revealed that the newly identified S601P mutated form of PDGFRA destabilizes the inactive conformation of the kinase domain that is necessary to bind imatinib as well as sorafenib. Conclusions:, We identified a novel mutation in FIP1L1-PDGFRA resulting in both imatinib and sorafenib resistance. The identification of novel drug-resistant FIP1L1-PDGFRA variants may help to develop the next generation of target-directed compounds for CEL/HES and other leukemias. [source] Ruthenium Complexes Containing Chiral N-Donor Ligands as Catalysts in Acetophenone Hydrogen Transfer , New Amino Effect on EnantioselectivityEUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 21 2005Montserrat Gómez Abstract New p -cymene ruthenium species containing chiral amino alcohols (1,3), primary (4,7) and secondary (8, 9) amino-oxazolines, were tested as catalysts in the hydrogen transfer of acetophenone, using 2-propanol as the hydrogen source. A remarkable effect on the enantioselectivity, but also on the activity, was observed depending on the amino-type oxazoline, Ru/8 and Ru/9 being low active and nonselective catalytic systems, in contrast to their primary counterpart Ru/5. Complexes containing amino-oxazolines (10,12) were prepared and fully characterized, both in solution and in solid state. The X-ray structure was determined for (SRu,RC)- 10. The diastereomeric ratios observed for complexes 10 and 11 were determined by 1H NMR and confirmed by means of structural modeling (semi-empirical PM3(tm) level). DFT theoretical calculations for the transition states involved in the hydrogen transfer process proved the important differences in their relative populations, which could justify the enantioselectivity divergences observed between primary and secondary amino-oxazoline ruthenium systems. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005) [source] Measuring Monetary Policy in Germany: A Structural Vector Error Correction ApproachGERMAN ECONOMIC REVIEW, Issue 3 2003Imke Brüggemann Monetary policy; cointegration; structural VAR analysis Abstract. A structural vector error correction (SVEC) model is used to investigate several monetary policy issues. While being data-oriented the SVEC framework allows structural modeling of the short-run and long-run properties of the data. The statistical model is estimated with monthly German data for 1975,98 where a structural break is detected in 1984. After splitting the sample, three stable long-run relations are found in each subsample which can be interpreted in terms of a money-demand equation, a policy rule and a relation for real output, respectively. Since the cointegration restrictions imply a particular shape of the long-run covariance matrix this information can be used to distinguish between permanent and transitory innovations in the estimated system. Additional restrictions are introduced to identify a monetary policy shock. [source] A New Farnesyl Diphosphate Synthase Gene from Taxus media Rehder: Cloning, Characterization and Functional ComplementationJOURNAL OF INTEGRATIVE PLANT BIOLOGY, Issue 6 2006Zhi-Hua Liao Abstract Farnesyl diphosphate synthase (FPS; EC 2.5.1.10) catalyzes the production of 15-carbon farnesyl diphosphate which is a branch-point intermediate for many terpenoids. This reaction is considered to be a rate-limiting step in terpenoid biosynthesis. Here we report for the first time the cloning of a new full-length cDNA encoding farnesyl diphosphate synthase from a gymnosperm plant species, Taxus media Rehder, designated as TmFPS1. The full-length cDNA of TmFPS1 (GenBank accession number: AY461811) was 1 464 bp with a 1 056-bp open reading frame encoding a 351-amino acid polypeptide with a calculated molecular weight of 40.3 kDa and a theoretical pI of 5.07. Bioinformatic analysis revealed that TmFPS1 contained all five conserved domains of prenyltransferases, and showed homology to other FPSs of plant origin. Phylogenetic analysis showed that farnesyl diphosphate synthases can be divided into two groups: one of prokaryotic origin and the other of eukaryotic origin. TmFPS1 was grouped with FPSs of plant origin. Homology-based structural modeling showed that TmFPS1 had the typical spatial structure of FPS, whose most prominent structural feature is the arrangement of 13 core helices around a large central cavity in which the catalytic reaction takes place. Our bioinformatic analysis strongly suggests that TmFPS1 is a functional gene. Southern blot analysis revealed that TmFPS1 belongs to a small FPS gene family in T. media. Northern blot analysis indicated that TmFPS1 is expressed in all tested tissues, including the needles, stems and roots of T. media. Subsequently, functional complementation with TmFPS1 in a FPS-deficient mutant yeast demonstrated that TmFPS1 did encode farnesyl diphosphate synthase, which rescued the yeast mutant. This study will be helpful in future investigations aiming at understanding the detailed role of FPS in terpenoid biosynthesis flux control at the molecular genetic level. (Managing editor: Wei Wang) [source] Conversion of trypsin to a functional threonine proteasePROTEIN SCIENCE, Issue 6 2006Teaster T. Baird Jr Abstract The hydroxyl group of a serine residue at position 195 acts as a nucleophile in the catalytic mechanism of the serine proteases. However, the chemically similar residue, threonine, is rarely used in similar functional context. Our structural modeling suggests that the Ser 195 , Thr trypsin variant is inactive due to negative steric interaction between the methyl group on the ,-carbon of Thr 195 and the disulfide bridge formed by cysteines 42 and 58. By simultaneously truncating residues 42 and 58 and substituting Ser 195 with threonine, we have successfully converted the classic serine protease trypsin to a functional threonine protease. Substitution of residue 42 with alanine and residue 58 with alanine or valine in the presence of threonine 195 results in trypsin variants that are 102,104 -fold less active than wild type in kcat/KM but >106 -fold more active than the Ser 195 , Thr single variant. The substitutions do not alter the substrate specificity of the enzyme in the P1,, P4, positions. Removal of the disulfide bridge decreases the overall thermostability of the enzyme, but it is partially rescued by the presence of threonine at position 195. [source] | |||||||||||||