3 resultados para BEADS

em Helda - Digital Repository of University of Helsinki


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The objective of the present study was to increase knowledge about the atelier culture of recent history, especially about the ways in which atelier clothes were made. I look at the ways of dress-making in the production of a renowned atelier, Salon Kaarlo Forsman. I also give a general outline of the atelier. The studying method I used was triangulation, which is a typical approach in case studies of recent history. My data include 23 dresses by the Salon Forsman, theme interviews of four of the Salon workers and one mannequin, data from my research work, as well as press material and archives. The basis of the analysis of these materials was a theme frame that I had put together with the help of pre-understanding. I then completed and defined the theme frame on the basis of the analysis of the data. I also analyzed the dresses in the fashion photos in the press material. Salon Kaarlo Forsman represents a certain cultural period, the years 1937-1986, and a place where a woman could have individual clothes made for her, from hats to fur coats. The atelier was particularly known for embroidery with beads, draping, and fantastic cuttings designed by the owner, fashion designer Kaarlo Forsman. I draw an outline of the work and practices of the atelier, but also that of Kaarlo Forsman’s life work, as he had a great influence on the sewing methods atelier clothes. Mr. Forsman was able to stretch the first period of modern fashion well into the third period by refusing new, labor-saving methods and sticking to individually designer clothes to the end of his enterprise. The crucial practices in the atelier that I present in this study are fitting, designing, finishing and sewing, as well as beading and the decoration of dresses. I compare the activity, practices and dress-making methods in the Forsman atelier to that of Haute Couture in Paris, which served as model for Finnish fashion houses. I point out the similarities and differences.

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The particles of Potato virus A (PVA; genus Potyvirus) are helically constructed filaments that contain multiple copies of a single type of coat-protein (CP) subunit and a single copy of genome-linked protein (VPg), attached to one end of the virion. Examination of negatively-stained virions by electron microscopy revealed flexuous, rod-shaped particles with no obvious terminal structures. It is known that particles of several filamentous plant viruses incorporate additional minor protein components, forming stable complexes that mediate particle disassembly, movement or transmission by insect vectors. The first objective of this work was to study the interaction of PVA movement-associated proteins with virus particles and how these interactions contribute to the morphology and function of the virus particles. Purified particles of PVA were examined by atomic force microscopy (AFM) and immuno-gold electron microscopy. A protrusion was found at one end of some of the potyvirus particles, associated with the 5' end of the viral RNA. The tip contained two virus-encoded proteins, the genome-linked protein (VPg) and the helper-component proteinase (HC-Pro). Both are required for cell-to-cell movement of the virus. Biochemical and electron microscopy studies of purified PVA samples also revealed the presence of another protein required for cell-to-cell movement the cylindrical inclusion protein (CI), which is also an RNA helicase/ATPase. Centrifugation through a 5-40% sucrose gradient separated virus particles with no detectable CI to a fraction that remained in the gradient, from the CI-associated particles that went to the pellet. Both types of particles were infectious. AFM and translation experiments demonstrated that when the viral CI was not present in the sample, PVA virions had a beads-on-a-string phenotype, and RNA within the virus particles was more accessible to translation. The second objective of this work was to study phosphorylation of PVA movement-associated and structural proteins (CP and VPg) in vitro and, if possible, in vivo. PVA virion structural protein CP is necessary for virus cell-to-cell movement. The tobacco protein kinase CK2 was identified as a kinase phosphorylating PVA CP. A major site of CK2 phosphorylation in PVA CP was identified as a single threonine within a CK2 consensus sequence. Amino acid substitutions affecting the CK2 consensus sequence in CP resulted in viruses that were defective in cell-to-cell and long-distance movement. The CK2 regulation of virion assembly and cell-to-cell movement by phosphorylation of CP was possibly due to the inhibition of CP binding to viral RNA. Four putative phosphorylation sites were identified from an in vitro phosphorylated recombinant VPg. All four were mutated and the spread of mutant viruses in two different host plants was studied. Two putative phosphorylation site mutants (Thr45 and Thr49) had phenotypes identical to that of a wild type (WT) virus infection in both Nicotiana benthamiana and N. tabacum plants. The other two mutant viruses (Thr132/Ser133 and Thr168) showed different phenotypes with increased or decreased accumulation rates, respectively, in inoculated and the first two systemically infected leaves of N. benthamiana. The same mutants were occasionally restricted to single cells in N. tabacum plants, suggesting the importance of these amino acids in the PVA infection cycle in N. tabacum.

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Single molecule force clamp experiments are widely used to investigate how enzymes, molecular motors, and other molecular mechanisms work. We developed a dual-trap optical tweezers instrument with real-time (200 kHz update rate) force clamp control that can exert 0–100 pN forces on trapped beads. A model for force clamp experiments in the dumbbell-geometry is presented. We observe good agreement between predicted and observed power spectra of bead position and force fluctuations. The model can be used to predict and optimize the dynamics of real-time force clamp optical tweezers instruments. The results from a proof-of-principle experiment in which lambda exonuclease converts a double-stranded DNA tether, held at constant tension, into its single-stranded form, show that the developed instrument is suitable for experiments in single molecule biology.