A review of floating semisubmersible hull systems:Column stabilized unit

Abstract Column stabilized semisubmersible is one of the most commonly used hull systems for the design and development of drilling and production platforms used for offshore deep water operations. Recent reconfiguration and design alterations have improved its hydrodynamic behaviour in rough weather conditions and, thus, its application and functionality in ocean engineering. Semisubmersible dry-trees applications and large wind turbine foundation systems in ultra-deep waters require high payload integration for reduced motion responses in all degrees of freedom. This paper presents a review of recent industrial and academic contributions to the development of column stabilized semisubmersible hulls used for deep water operations. It also provides an overview of the motion and structural attachments of semisubmersibles. The type and formation of dry-trees semisubmersibles are discussed. The dynamic behaviour and comparative advantages of them are also explained

Comparative analysis of Musaceae species based on the cluster composition.

<p>(A) Sequence composition of the largest clusters is shown. The size of the rectangle is proportional to the number of reads in a cluster for each species. Bar plot in the top row shows the size of the clusters as number of reads. Color of the rectangles correspond to the type of the repeat. Upper lines label groups of clusters discussed in the text. The percentage of reads included in the group is shown in parentheses. (B) The presence of mobile element protein domains in the contig assembled from sequences within the cluster. Only clusters that were annotated are shown. (C–E) Validation of clustering results by Southern blot. Genomic DNA from 15 species was probed with sequences derived from clusters CL16, CL51. and CL30. The lanes contain DNA from 1/<i>M. acuminata</i> ssp. <i>zebrina</i> (ITC 0728), 2/<i>M. acuminata</i> ssp. <i>malaccensis</i> (ITC 0250), 3/<i>M. acuminata</i> ssp. <i>burmannicoides</i> (ITC 0249), 4/<i>M. ornata</i> (ITC 0637), 5/<i>M. mannii</i> (ITC 1411), 6/<i>M. ornata</i> (ITC 0528), 7/<i>M. balbisiana</i> (ITC 1120), 8/<i>M. balbisiana</i> (‘Pisang Klutuk Wulung’), 9/<i>M. balbisiana</i> (ITC 0247), 10/<i>M. peekelii</i> (ITC 0917), 11/<i>M. maclayi</i> (ITC 0614), 12/<i>M. textilis</i> (ITC 0539), 13/<i>M. beccarii</i> (ITC 1070), 14/<i>E. ventricosum</i> (ITC 1387), and 15/<i>E. gilletii</i> (ITC 1389).</p

Genome proportions of repetitive sequences.

<p>Genome proportions of repetitive sequences.</p

Evolutionary relationship between species of Musaceae family.

<p>Phylogeny estimated from ITS data using BioNJ. Six genomes selected for repeat analysis are highlighted.</p

Sequenced species.

<p>Sequenced species.</p

Variability of sequences within cluster CL18.

<p>(A) Sequence reads are represented by nodes of the graph and reads with identity of at least 90% with minimal overlap of 110 nt are connected by lines. Graph layout was calculated using the 3D version of the Fruchterman and Reingold algorithm <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0098918#pone.0098918-Fruchterman1" target="_blank">[55]</a> from which a 2D projection is shown. Reads are colored based on their similarity to conserved coding domains of LTR retrotransposons. Reads from LTR regions are colored by light blue. (B) Nodes of the graph are colored based on their species of origin. The six identical graphs show reads derived from each species in red; remaining reads are gray to highlight species-specific parts of the graphs. The parts of the graphs that represent the most variable sequence regions in CRM CL18 element, which can differentiate between species, are labeled by black arrows. (C) Maximum-likelihood tree based on nucleotide alignment of sequences covering the reverse transcriptase protein domain of CRM CL18. Sequence read names are colored based on the species of origin.</p

Comparison of genomic abundance of analyzed reads in all six species.

<p>(A–O) Scatter plots show pairwise comparisons of all analyzed sequences between pairs of species. Each spot corresponds to one sequence read. For each sequence read, the number of similarity hits in each species is displayed (this number is proportional to genomic representation of a particular sequence). Red diagonal line marks the position of sequences with equiproportional genomic representations. Sequences with differential genomic representation between species deviate from diagonal. The 45S rDNA sequences are shown in red. (P) Graph summarizing the number of identified read similarities between and within genomes. Width of the lines connecting nodes of the graph correspond to the number of identified similarity hits between sequence reads from different species (straight lines) and within the same species (loops).</p

Analysis of 100-Pahang assembly using Profrep.

<p>Genomic sequence Chr9:20,150,000–20,250,000 together with repeat annotation was obtained from the Banana Genome Hub (<a href="http://banana-genome.cirad.fr/" target="_blank">http://banana-genome.cirad.fr/</a>) and analyzed using the Profrep tool against our Musaceae repetitive sequence databases. (A) Six tracks show the numbers of similarity hits against reads from six Musaceae genomes as calculated by Profrep. (B) Annotation of genomic region based on our <i>M. acuminata</i> repeat annotation and Profrep analysis. (C) Annotation of repeats in the DH-Pahang genome obtained from the Banana Genome Hub.</p

Identification of NM1 interacting proteins in the cytosol.

<p>Digitonin extract from suspension HeLa cells was incubated with recombinant Str-IQ12-His peptide containing N-terminal OneStrep tag (IQ12) and Streptactin beads as a control for background binding. Bound proteins were resolved on 4–20% SDS-PAGE gel and stained with SimplyBlue. Mass spectrometric analysis of the protein bands that co-purified with bait (arrows) identified importin 5 and heat shock protein 90 beta (HSP90) (<b>A</b>). SimplyBlue stained 4–20% SDS-PAGE gel with proteins that interacted with Str-GFP-NM1-(Q123.T) and Str-GFP as a control in digitonin extract of HEK293T cells. The arrows show positions of bands that contained proteins identified using mass spectrometry as importin 5, importin 7, importin-β1, HSP90 beta and calmodulin (<b>B</b>). Proteins that co-immunoprecipitate with antibody to endogenous NM1 from HeLa extracts were resolved using SDS-PAGE and tranferred onto nitrocelulose membrane. Membrane was probed with with anti-NM1, anti-importin 5 (IPO5), anti-importin 7 (IPO7), anti-importin-β1 (KPNB1). Rabbit polyclonal antibody against GFP was used as a control for backgroung binding (<b>C</b>). N-terminally Strep tagged GFP-NM1-(Q123.T) ^NLSwt (wt), GFP-NM1-(Q123.T) ^NLSmut (mut) and GFP as negative control (nc) were expressed in HEK293T cells. Cells were extracted with buffer containing digitonin (digi) to obtain soluble cytosol; pellet was re-extracted with the same buffer containing 1% Triton X-100 (triton). Bound proteins were resolved on SDS-PAGE, transferred to nitrocelulose. Membrane was incubated with antibody to importin 5 ans GFP (<b>D</b>). Beads containing Str-GFP-NM1-(Q123.T) and Str-GFP-SV40 NLS and associated proteins were eluted first with buffer containing GTP-loaded RanQ69L or buffer alone and then with biotin containig buffer that liberated Strep-tagged bait proteins from the column. Proteins eluted from the beads were resolved on SDS-PAGE and transferred to nitrocelulose membrane. GFP, importin 5 and importin-β1 signals were detected using specific antibodies (<b>E</b>). Signal from secondary antibodies was detected using LI-COR Odyssey infrared imaging system.</p

Mutation of basic residues in the neck of NM1/Myo1c abolishes its nuclear import.

<p>U2OS cells were transfected with full length NM1-V5/His (<b>A</b>), NM1-V5/His lacking the second IQ motif (<b>B</b>), and NM1-V5/His with point mutation of basic amino acids within the NLS into alanines (<b>C</b>). Below the pictures are schematic representations of constructs used. Color coding is the same as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0030529#pone-0030529-g002" target="_blank"><b>Fig. 2</b></a>. Cells were fixed 48 hours post transfection and labeled with anti-V5 antibody, pictures were obtained using wide-field microscope, scale bar: 10 µm (<b>D</b>) U2OS cells transiently transfected with Myo1c-V5/His show nuclear localization of the protein Picture is a single confocal plane, obtained by confocal microscope. Scale bar: 10 µm. (<b>E</b>) Nuclear and cytosolic extracts were prepared from liver of either wild type (WT) or NM1 knock-out (KO) mice. Equal amount of protein was resolved using SDS-PAGE and electro-transferred to nitrocellulose. Membrane was probed with anti-NM1, anti-Myo1c, anti hnRNP C1/C2 and GAPDH antibody. Signal was detected using LI-COR Odyssey infrared imaging system. (<b>F</b>) U2OS cells were transiently transfected with Myo1c-V5/His. 24 hours after transfection cells were treated with nocodazole or aphidicolin to stall the cells either in G2/M or in G1/S phase of cell cycle. After the release from the block cells were cultivated for another 24 hours. Samples were taken in indicated timepoints. Cells were labeled with antibody to V5 tag, patterns counted and divided into three groups according to the localization of fluorescent proteins. More than 100 cells were counted in each timepoint, expreriment was repeated twice with similar result.</p