Calibration procedures and first data set of Southern Ocean chlorophyll a profiles collected by elephant seals equipped with a newly developed CTD-fluorescence tags

In-situ observation of the marine environment has traditionally relied on ship-based platforms. The obvious consequence is that physical and biogeochemical properties have been dramatically undersampled, especially in the remote Southern Ocean (SO). The difficulty in obtaining in situ data represents the major limitations to our understanding, and interpretation of the coupling between physical forcing and the biogeochemical response. Southern elephant seals (Mirounga leonina) equipped with a new generation of oceanographic sensors can measure ocean structure in regions and seasons rarely observed with traditional oceanographic platforms. Over the last few years, seals have allowed for a considerable increase in temperature and salinity profiles from the SO. However we were still lacking information on the spatio-temporal variation of phytoplankton concentration. This information is critical to assess how the biological productivity of the SO, with direct consequences on the amount of CO2 "fixed" by the biological pump, will respond to global warming. In this research program, we use an innovative sampling fluorescence approach to quantify phytoplankton concentration at sea. For the first time, a low energy consumption fluorometer was added to Argos CTD-SRDL tags, and these novel instruments were deployed on 27 southern elephant seals between 25 December 2007 and the 4 February 2011. As many as 3388 fluorescence profiles associated with temperature and salinity measurements were thereby collected from a vast sector of the Southern Indian Ocean. This paper address the calibration issue of the fluorometer before being deployed on elephant seals and present the first results obtained for the Indian Sector of the Southern Ocean.This in situ system is implemented in synergy with satellite ocean colour radiometry. Satellite-derived data is limited to the surface layer and is restricted over the SO by extensive cloud cover. However, with the addition of these new tags, we're able to assess the 3 dimension distribution of phytoplankton concentration by foraging southern elephant seals. This approach reveals that for the Indian sector of the SO, the surface chlorophyll a (chl a) concentrations provided by MODIS were underestimated by a factor of the order of 2–3 compared to in situ measurements. The scientific outcomes of this program include an improved understanding of both the present state and variability in ocean biology, and the accompanying biogeochemistry, as well as the delivery of real-time and open-access data to scientists

Transmembrane but not soluble helices fold inside the ribosome tunnel

Integral membrane proteins are assembled into the ER membrane via a continuous ribosome-translocon channel. The hydrophobicity and thickness of the core of the membrane bilayer leads to the expectation that transmembrane (TM) segments minimize the cost of harbouring polar polypeptide backbones by adopting a regular pattern of hydrogen bonds to form α-helices before integration. Co-translational folding of nascent chains into an α-helical conformation in the ribosomal tunnel has been demonstrated previously, but the features governing this folding are not well understood. In particular, little is known about what features influence the propensity to acquire α-helical structure in the ribosome. Using in vitro translation of truncated nascent chains trapped within the ribosome tunnel and molecular dynamics simulations, we show that folding in the ribosome is attained for TM helices but not for soluble helices, presumably facilitating SRP (signal recognition particle) recognition and/or a favourable conformation for membrane integration upon translocon entry

Determining Peptide Partitioning Properties via Computer Simulation

The transfer of polypeptide segments into lipid bilayers to form transmembrane helices represents the crucial first step in cellular membrane protein folding and assembly. This process is driven by complex and poorly understood atomic interactions of peptides with the lipid bilayer environment. The lack of suitable experimental techniques that can resolve these processes both at atomic resolution and nanosecond timescales has spurred the development of computational techniques. In this review, we summarize the significant progress achieved in the last few years in elucidating the partitioning of peptides into lipid bilayer membranes using atomic detail molecular dynamics simulations. Indeed, partitioning simulations can now provide a wealth of structural and dynamic information. Furthermore, we show that peptide-induced bilayer distortions, insertion pathways, transfer free energies, and kinetic insertion barriers are now accurate enough to complement experiments. Further advances in simulation methods and force field parameter accuracy promise to turn molecular dynamics simulations into a powerful tool for investigating a wide range of membrane active peptide phenomena

Membrane Docking Geometry of GRP1 PH Domain Bound to a Target Lipid Bilayer: An EPR Site-Directed Spin-Labeling and Relaxation Study

The second messenger lipid PIP3 (phosphatidylinositol-3,4,5-trisphosphate) is generated by the lipid kinase PI3K (phosphoinositide-3-kinase) in the inner leaflet of the plasma membrane, where it regulates a broad array of cell processes by recruiting multiple signaling proteins containing PIP3-specific pleckstrin homology (PH) domains to the membrane surface. Despite the broad importance of PIP3-specific PH domains, the membrane docking geometry of a PH domain bound to its target PIP3 lipid on a bilayer surface has not yet been experimentally determined. The present study employs EPR site-directed spin labeling and relaxation methods to elucidate the membrane docking geometry of GRP1 PH domain bound to bilayer-embedded PIP3. The model target bilayer contains the neutral background lipid PC and both essential targeting lipids: (i) PIP3 target lipid that provides specificity and affinity, and (ii) PS facilitator lipid that enhances the PIP3 on-rate via an electrostatic search mechanism. The EPR approach measures membrane depth parameters for 18 function-retaining spin labels coupled to the PH domain, and for calibration spin labels coupled to phospholipids. The resulting depth parameters, together with the known high resolution structure of the co-complex between GRP1 PH domain and the PIP3 headgroup, provide sufficient constraints to define an optimized, self-consistent membrane docking geometry. In this optimized geometry the PH domain engulfs the PIP3 headgroup with minimal bilayer penetration, yielding the shallowest membrane position yet described for a lipid binding domain. This binding interaction displaces the PIP3 headgroup from its lowest energy position and orientation in the bilayer, but the headgroup remains within its energetically accessible depth and angular ranges. Finally, the optimized docking geometry explains previous biophysical findings including mutations observed to disrupt membrane binding, and the rapid lateral diffusion observed for PIP3-bound GRP1 PH domain on supported lipid bilayers

A simple compact model to analyze the impact of ballistic and quasi-ballistic transport on ring oscillator performance

IEEE International Conference on Integrated Circuit Design and Technology, Grenoble, FRANCE, JUN 02-04, 2008International audienceThis paper presents an analytical modeling of ballistic and quasi-ballistic transport, implemented in Verilog-A environment and used for circuit simulation. Our model is based on the Lundstrom's approach and uses an expression of the backscattering coefficient given by the flux method. The model takes also into account short channel effects and tales into account the effects of different scattering processes through a dynamical mean free path. Using this model, CMOS inverters and ring oscillators have been simulated to highlight the impact of ballistic and quasi-ballistic transport on static and transient performance

Influence of Defects on the Schottky Barrier Height at BaTiO₃/RuO₂ Interfaces

The Schottky barrier formation between polycrystalline acceptor‐doped BaTiO₃ and high work function RuO₂ is studied using photoelectron spectroscopy. Schottky barrier heights for electrons of ≈1.4 eV are determined, independent of doping level and oxygen vacancy concentration of the substrates. The insensitivity of the barrier height is related to the high permittivity of BaTiO₃, which results in space‐charge regions (SCRs) being considerably wider than the inelastic mean free path of the photoelectrons. SCRs at any kind of interface should, therefore, be more important for the electronic and ionic conductivities in BaTiO₃ than in materials with lower permittivity. A Ba‐rich phase at the surface of reduced acceptor‐doped BaTiO₃ is also identified, which is explained by the formation of Ti vacancies in the 2D electron gas region at the surface