Accuracy of wind observations from open-ocean buoys: Correction for flow distortion

The comparison of equivalent neutral winds obtained from (a) four WHOI buoys in the subtropics and (b) scatterometer estimates at those locations reveals a root-mean-square (RMS) difference of 0.56-0.76 m/s. To investigate this RMS difference, different buoy wind error sources were examined. These buoys are particularly well suited to examine two important sources of buoy wind errors because: (1) redundant anemometers and a comparison with numerical flow simulations allow us to quantitatively assess flow distortion errors, and (2) one-minute sampling at the buoys allows us to examine the sensitivity of buoy temporal sampling/averaging in the buoy-scatterometer comparisons. The inter-anemometer difference varies as a function of wind direction relative to the buoy wind vane and is consistent with the effects of flow distortion expected based on numerical flow simulations. Comparison between the anemometers and scatterometer winds supports the interpretation that the inter-anemometer disagreement, which can be up to 5% of the wind speed, is due to flow distortion. These insights motivate an empirical correction to the individual anemometer records and subsequent comparison with scatterometer estimates show good agreement

Structure of the PUD-1 and PUD-2 heterodimer.

<p>(<b>A</b>) Ribbon representation of the PUD-1 and PUD-2 heterodimer in cross-eye stereoview. PUD-1 is green and PUD-2 is cyan. The β-strands are labeled with numbers and the N and C termini are indicated. (<b>B</b>) Structural superposition of PUD-1 and PUD-2 subunit. (<b>C</b>) Interactions at the dimer interface. For clarity, only residues at the interface are shown for PUD-1. Oxygen is red, nitrogen is blue, sulfur is orange and carbon is green for PUD-1 and cyan for PUD-2. Hydrogen bonds are shown as yellow dashed lines. (<b>D</b>) Conserved surface. The ribbon and surface representations of PUD-1 structure are shown side-by-side and in two opposite orientations. The residues conserved in 100% and 80% of the 31 homologs of PUD-1 and PUD-2, as shown in Figure S7, are colored orange and yellow, respectively, for side chain atoms. (<b>E</b>) Sequence alignment of the PUD family proteins in <i>C. elegans</i>. Residues with 100% and 80% conservation are shaded with black and grey, respectively. The secondary structures observed in the crystal structure are shown on the top for PUD-2 and at the bottom for PUD-1. Residues whose surface area is buried by 10-30 Ų and at least 30 Ų upon dimerization are denoted by open and solid circles, respectively.</p

<i>hq6</i> animals are more resistant to Aβ(1-42) toxicity.

<p>(<b>A</b>) In either WT or <i>daf-2</i>(<i>RNAi</i>) background, <i>hq6</i> conferred resistance to paralysis induced by <i>dvIs2</i>, which expressed Aβ(1-42) in the body wall muscles (N ≥83, representative of three experiments). (<b>B</b>) <i>hq6</i> increased the brood size of <i>dvIs2</i> worms (N ≥10, representative of three experiments). (<b>C</b>-<b>D</b>) <i>tm6107;hq6</i> and <i>tm5053; hq6</i> double mutants showed similar resistance to Aβ toxicity as the <i>hq6</i> single mutant.</p

Expression patterns of the paralogs of PUD-1 and PUD-2 in <i>C. elegans.</i>

<p>(<b>A</b>-D) Distributions of the PUD-3, PUD-4, PUDL-1, and PUDL-2 translational GFP fusion proteins, respectively.</p

PUD-1 and PUD-2 form a heterodimer.

<p>(<b>A</b>) FLAG IP followed by MS analysis identified HSP-1 and PUD-2 as binding proteins associated with FLAG-PUD-1. Shown is the silver stained gel of the IP products before MS analysis. (<b>B</b>) Purified recombinant PUD-1 and PUD-2 can be cross-linked together and the cross-linked species seems to be a heterodimer. (<b>C</b>) The PUD-1 and PUD-2 heterodimer, each with a SMT3 tag, was also observed by gel filtration. (<b>D</b>) Gel filtration analysis of the <i>C. elegans</i> PUD gene family proteins. SMT3 tagged proteins were loaded onto a Superdex-200 10/300 column individually or in indicated combinations.</p

Expression of <i>P</i>_<i>pud-1</i><i>::GFP::pud-1</i> and <i>P</i>_<i>pud-2</i><i>::GFP::pud-2</i> from single-copy transgenes inserted into the <i>C. elegans</i> genome.

<p>PUD-1 (<b>A</b>, <b>B</b>, <b>E</b>) and PUD-2 (<b>C</b>, <b>D</b>, <b>F</b>) are both expressed the intestine (arrowheads) and hypodermis (long arrow). In the intestinal cells, PUD-1 (<b>B</b>) and PUD-2 (<b>D</b>) are distributed diffusely in the cytoplasm and the nucleoplasm, and largely excluded from the nucleolus (short arrow) expect for one or more nuclear puncta. The nucleolar GFP puncta are more distinct in high-copy transgenic strains (Figure S1). PUD-1 (<b>E</b>) and PUD-2 (<b>F</b>) are both localized in the hypodermal fibrous organelles with a characteristic circumferential orientation.</p